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data-component-name="ProfileCheckPaperUpdate" data-props="{}" data-trace="false" data-dom-id="ProfileCheckPaperUpdate-react-component-7b37631b-6114-46c9-8968-7d9af13be029"></div> <div id="ProfileCheckPaperUpdate-react-component-7b37631b-6114-46c9-8968-7d9af13be029"></div> <div class="DesignSystem"><div class="onsite-ping" id="onsite-ping"></div></div><div class="profile-user-info DesignSystem"><div class="social-profile-container"><div class="left-panel-container"><div class="user-info-component-wrapper"><div class="user-summary-cta-container"><div class="user-summary-container"><div class="social-profile-avatar-container"><img class="profile-avatar u-positionAbsolute" border="0" alt="" src="//a.academia-assets.com/images/s200_no_pic.png" /></div><div class="title-container"><h1 class="ds2-5-heading-sans-serif-sm">Buz Barstow</h1><div class="affiliations-container fake-truncate js-profile-affiliations"><div><a class="u-tcGrayDarker" href="https://hms-harvard.academia.edu/">Harvard 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translate="no">done</span>Following</button></div></div><div class="user-stats-container"><a><div class="stat-container js-profile-followers"><p class="label">Followers</p><p class="data">8</p></div></a><a><div class="stat-container js-profile-followees" data-broccoli-component="user-info.followees-count" data-click-track="profile-expand-user-info-following"><p class="label">Following</p><p class="data">1</p></div></a><div class="js-mentions-count-container" style="display: none;"><a href="/BuzBarstow/mentions"><div class="stat-container"><p class="label">Mentions</p><p class="data"></p></div></a></div><span><div class="stat-container"><p class="label"><span class="js-profile-total-view-text">Public Views</span></p><p class="data"><span class="js-profile-view-count"></span></p></div></span></div><div class="user-bio-container"><div class="profile-bio fake-truncate js-profile-about" style="margin: 0px;"><b>Address: </b>Cambridge, Massachusetts, United States<br /><div class="js-profile-less-about u-linkUnstyled u-tcGrayDarker u-textDecorationUnderline u-displayNone">less</div></div></div><div class="suggested-academics-container"><div class="suggested-academics--header"><p class="ds2-5-body-md-bold">Related Authors</p></div><ul class="suggested-user-card-list"><div class="suggested-user-card"><div class="suggested-user-card__avatar social-profile-avatar-container"><a href="https://unizg.academia.edu/AndrejDujella"><img class="profile-avatar u-positionAbsolute" alt="Andrej Dujella" border="0" onerror="if (this.src != '//a.academia-assets.com/images/s200_no_pic.png') this.src = '//a.academia-assets.com/images/s200_no_pic.png';" width="200" height="200" src="https://0.academia-photos.com/29857/9709/9189/s200_andrej.dujella.jpg" /></a></div><div class="suggested-user-card__user-info"><a class="suggested-user-card__user-info__header ds2-5-body-sm-bold ds2-5-body-link" href="https://unizg.academia.edu/AndrejDujella">Andrej Dujella</a><p class="suggested-user-card__user-info__subheader ds2-5-body-xs">University of Zagreb</p></div></div><div class="suggested-user-card"><div class="suggested-user-card__avatar social-profile-avatar-container"><a href="https://uppsala.academia.edu/HeminKoyi"><img class="profile-avatar u-positionAbsolute" alt="Hemin Koyi" border="0" onerror="if (this.src != '//a.academia-assets.com/images/s200_no_pic.png') this.src = '//a.academia-assets.com/images/s200_no_pic.png';" width="200" height="200" src="https://0.academia-photos.com/102248/28141/11213115/s200_hemin.koyi.jpg" /></a></div><div class="suggested-user-card__user-info"><a class="suggested-user-card__user-info__header ds2-5-body-sm-bold ds2-5-body-link" href="https://uppsala.academia.edu/HeminKoyi">Hemin Koyi</a><p class="suggested-user-card__user-info__subheader ds2-5-body-xs">Uppsala University</p></div></div><div class="suggested-user-card"><div class="suggested-user-card__avatar social-profile-avatar-container"><a href="https://uel.academia.edu/JanaJavornik"><img class="profile-avatar u-positionAbsolute" alt="Jana Javornik" border="0" onerror="if (this.src != '//a.academia-assets.com/images/s200_no_pic.png') this.src = '//a.academia-assets.com/images/s200_no_pic.png';" width="200" height="200" src="https://0.academia-photos.com/113072/30527/13170018/s200_jana.javornik.jpg" /></a></div><div class="suggested-user-card__user-info"><a class="suggested-user-card__user-info__header ds2-5-body-sm-bold ds2-5-body-link" href="https://uel.academia.edu/JanaJavornik">Jana Javornik</a><p class="suggested-user-card__user-info__subheader ds2-5-body-xs">University of East London</p></div></div><div class="suggested-user-card"><div class="suggested-user-card__avatar social-profile-avatar-container"><a href="https://leicester.academia.edu/GrahamMartin"><img class="profile-avatar u-positionAbsolute" alt="Graham Martin" border="0" onerror="if (this.src != '//a.academia-assets.com/images/s200_no_pic.png') this.src = 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href="https://usal.academia.edu/GabrielGutierrezAlonso">Gabriel Gutierrez-Alonso</a><p class="suggested-user-card__user-info__subheader ds2-5-body-xs">University of Salamanca</p></div></div><div class="suggested-user-card"><div class="suggested-user-card__avatar social-profile-avatar-container"><a href="https://mq.academia.edu/JohnSutton"><img class="profile-avatar u-positionAbsolute" alt="John Sutton" border="0" onerror="if (this.src != '//a.academia-assets.com/images/s200_no_pic.png') this.src = '//a.academia-assets.com/images/s200_no_pic.png';" width="200" height="200" src="https://0.academia-photos.com/176044/43811/40295/s200_john.sutton.jpg" /></a></div><div class="suggested-user-card__user-info"><a class="suggested-user-card__user-info__header ds2-5-body-sm-bold ds2-5-body-link" href="https://mq.academia.edu/JohnSutton">John Sutton</a><p class="suggested-user-card__user-info__subheader ds2-5-body-xs">Macquarie University</p></div></div><div class="suggested-user-card"><div class="suggested-user-card__avatar social-profile-avatar-container"><a href="https://ufrgs.academia.edu/ErosCarvalho"><img class="profile-avatar u-positionAbsolute" alt="Eros Carvalho" border="0" onerror="if (this.src != '//a.academia-assets.com/images/s200_no_pic.png') this.src = '//a.academia-assets.com/images/s200_no_pic.png';" width="200" height="200" src="https://0.academia-photos.com/176585/88715/48865541/s200_eros.carvalho.jpg" /></a></div><div class="suggested-user-card__user-info"><a class="suggested-user-card__user-info__header ds2-5-body-sm-bold ds2-5-body-link" href="https://ufrgs.academia.edu/ErosCarvalho">Eros Carvalho</a><p class="suggested-user-card__user-info__subheader ds2-5-body-xs">Universidade Federal do Rio Grande do Sul</p></div></div><div class="suggested-user-card"><div class="suggested-user-card__avatar social-profile-avatar-container"><a href="https://swansea.academia.edu/KevinArbuckle"><img class="profile-avatar u-positionAbsolute" alt="Kevin Arbuckle" border="0" onerror="if (this.src != '//a.academia-assets.com/images/s200_no_pic.png') this.src = '//a.academia-assets.com/images/s200_no_pic.png';" width="200" height="200" src="https://0.academia-photos.com/191329/90380/6936137/s200_kevin.arbuckle.jpg" /></a></div><div class="suggested-user-card__user-info"><a class="suggested-user-card__user-info__header ds2-5-body-sm-bold ds2-5-body-link" href="https://swansea.academia.edu/KevinArbuckle">Kevin Arbuckle</a><p class="suggested-user-card__user-info__subheader ds2-5-body-xs">Swansea University</p></div></div><div class="suggested-user-card"><div class="suggested-user-card__avatar social-profile-avatar-container"><a href="https://ku-dk.academia.edu/JesperHoffmeyer"><img class="profile-avatar u-positionAbsolute" alt="Jesper Hoffmeyer" border="0" onerror="if (this.src != '//a.academia-assets.com/images/s200_no_pic.png') this.src = '//a.academia-assets.com/images/s200_no_pic.png';" width="200" height="200" src="https://0.academia-photos.com/241162/92724/102335/s200_jesper.hoffmeyer.jpg" /></a></div><div class="suggested-user-card__user-info"><a class="suggested-user-card__user-info__header ds2-5-body-sm-bold ds2-5-body-link" href="https://ku-dk.academia.edu/JesperHoffmeyer">Jesper Hoffmeyer</a><p class="suggested-user-card__user-info__subheader ds2-5-body-xs">University of Copenhagen</p></div></div></ul></div></div></div><div class="right-panel-container"><div class="user-content-wrapper"><div class="uploads-container" id="social-redesign-work-container"><div class="upload-header"><h2 class="ds2-5-heading-sans-serif-xs">Uploads</h2></div><div class="documents-container backbone-social-profile-documents" style="width: 100%;"><div class="u-taCenter"></div><div class="profile--tab_content_container js-tab-pane tab-pane active" id="all"><div class="profile--tab_heading_container js-section-heading" data-section="Papers" id="Papers"><h3 class="profile--tab_heading_container">Papers by Buz Barstow</h3></div><div class="js-work-strip profile--work_container" data-work-id="29586679"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" rel="nofollow" href="https://www.academia.edu/29586679/Molecular_Mechanisms_for_the_Biological_Storage_of_Renewable_Energy"><img alt="Research paper thumbnail of Molecular Mechanisms for the Biological Storage of Renewable Energy" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" rel="nofollow" href="https://www.academia.edu/29586679/Molecular_Mechanisms_for_the_Biological_Storage_of_Renewable_Energy">Molecular Mechanisms for the Biological Storage of Renewable Energy</a></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="29586679"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="29586679"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 29586679; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=29586679]").text(description); $(".js-view-count[data-work-id=29586679]").attr('title', description).tooltip(); }); 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"profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="29586678"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" rel="nofollow" href="https://www.academia.edu/29586678/Rapid_Construction_of_a_Whole_genome_Transposon_Insertion_Collection_for_Shewanella_oneidensis_by_Knockout_Sudoku"><img alt="Research paper thumbnail of Rapid Construction of a Whole-genome Transposon Insertion Collection for Shewanella oneidensis by Knockout Sudoku" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" rel="nofollow" href="https://www.academia.edu/29586678/Rapid_Construction_of_a_Whole_genome_Transposon_Insertion_Collection_for_Shewanella_oneidensis_by_Knockout_Sudoku">Rapid Construction of a Whole-genome Transposon Insertion Collection for Shewanella oneidensis by Knockout Sudoku</a></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="29586678"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="29586678"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 29586678; 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})(["https://a.academia-assets.com/assets/wow_profile-a9bf3a2bc8c89fa2a77156577594264ee8a0f214d74241bc0fcd3f69f8d107ac.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (false){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "-1" } } $('.js-work-strip[data-work-id=29586678]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":29586678,"title":"Rapid Construction of a Whole-genome Transposon Insertion Collection for Shewanella oneidensis by Knockout Sudoku","internal_url":"https://www.academia.edu/29586678/Rapid_Construction_of_a_Whole_genome_Transposon_Insertion_Collection_for_Shewanella_oneidensis_by_Knockout_Sudoku","owner_id":5103660,"coauthors_can_edit":true,"owner":{"id":5103660,"first_name":"Buz","middle_initials":null,"last_name":"Barstow","page_name":"BuzBarstow","domain_name":"hms-harvard","created_at":"2013-08-11T09:43:28.377-07:00","display_name":"Buz Barstow","url":"https://hms-harvard.academia.edu/BuzBarstow"},"attachments":[]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="29586666"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/29586666/First_studies_for_a_low_temperature_higher_order_mode_absorber_for_the_Cornell_ERL_prototype"><img alt="Research paper thumbnail of First studies for a low temperature higher-order-mode absorber for the Cornell ERL prototype" class="work-thumbnail" src="https://attachments.academia-assets.com/50029709/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/29586666/First_studies_for_a_low_temperature_higher_order_mode_absorber_for_the_Cornell_ERL_prototype">First studies for a low temperature higher-order-mode absorber for the Cornell ERL prototype</a></div><div class="wp-workCard_item"><span>Proceedings of the 2003 Bipolar/BiCMOS Circuits and Technology Meeting (IEEE Cat. No.03CH37440)</span><span>, 2003</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Cornell University, in collaboration with Jefferson Laboratory, has proposed the construction of ...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Cornell University, in collaboration with Jefferson Laboratory, has proposed the construction of a prototype energyrecovery linac (ERL) to study the energy recovery concept with high current, low emittance beams . The beam with a current of up to 100 mA will excite significant higher-order-mode (HOM) power in the superconducting (s.c.) RF cavities with frequencies up to 100 GHz. Strong damping of the HOMs is essential for beam stability and to reduce the HOM losses to a few hundred Watts per meter. To achieve this demanding goal we plan to place RF absorbing material in the beam tubes between the cavities in the linac. However, this will require operating the HOM absorbers at temperatures below 80 K to simplify the thermal transition to the cavities at 2 K with low static losses to 2 K. One possible material candidate is ferrite, as it is used at room temperature in the HOM absorbers in the s.c. CESR cavities. In this paper we present experiments performed to study the RF absorption properties of ferrite at cryogenic temperatures in the frequency range from 1 GHz to 15 GHz. First results are shown and the resulting HOM damping is evaluated and discussed. 0-7803-7739-9</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="72253f4a7f60f3b5767a61b45afe4af1" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":50029709,"asset_id":29586666,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/50029709/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="29586666"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="29586666"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 29586666; 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="29586664"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/29586664/Overview_of_the_cornell_ERL_injector_cryomodule"><img alt="Research paper thumbnail of Overview of the cornell ERL injector cryomodule" class="work-thumbnail" src="https://attachments.academia-assets.com/50029704/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/29586664/Overview_of_the_cornell_ERL_injector_cryomodule">Overview of the cornell ERL injector cryomodule</a></div><div class="wp-workCard_item"><span>Proceedings of the 2003 Bipolar/BiCMOS Circuits and Technology Meeting (IEEE Cat. No.03CH37440)</span><span>, 2003</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">The Laboratory for Elementary-Particle Physics, Cornell University, in collaboration with Jeffers...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">The Laboratory for Elementary-Particle Physics, Cornell University, in collaboration with Jefferson Lab is exploring the potential of a Synchrotron Radiation User Facility based on a multi-GeV, low emittance, Energy-Recovery Linac (ERL) with a 100 mA CW beam[1]. The ERL injector will accelerate bunches from the electron source from 0.5 MeV to 5 MeV with minimal emittance growth. The injector and main linac of the ERL will be based on superconducting RF technology to provide CW operation. There will be one cryomodule with five 1300 MHz 2-cell cavities, each providing one MV of acceleration, corresponding to an accelerating field of about 4.3 MV/m in CW operation. Besides standard features such as an integrated helium vessel and mechanical tuner, each cavity has two input couplers, symmetrically placed on the beam pipe to cancel kicks due to coupler fields. For a 100 mA maximum injected beam current, each coupler must deliver 50 kW of beam power leading to a Qext of 4.6 x10 4 for matched beam loading conditions. Antenna-and loop-based HOM couplers can disturb beam emittance through kicks. We plan to avoid the use of such couplers. Following the strategy for B-factory SRF cavities, the beam pipe aperture has been enlarged on one side to propagate all higher order modes out to symmetric ferrite beam pipe loads. These are positioned outside the helium vessel and cooled to liquid nitrogen temperature. Ferrite properties at 77 K have been measured and the corresponding damping evaluated. To explore the full capabilities of the injector, energy gains up to 3 MV per cavity will be considered at lower beam currents. For this flexibility, the input coupling needs to be adjustable by a factor of 9.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="ca962725e5e59f39df479dfe53898b6a" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":50029704,"asset_id":29586664,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/50029704/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="29586664"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="29586664"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 29586664; 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="29586662"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/29586662/The_Cornell_ERL_prototype_project"><img alt="Research paper thumbnail of The Cornell ERL prototype project" class="work-thumbnail" src="https://attachments.academia-assets.com/50029712/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/29586662/The_Cornell_ERL_prototype_project">The Cornell ERL prototype project</a></div><div class="wp-workCard_item"><span>Proceedings of the 2003 Bipolar/BiCMOS Circuits and Technology Meeting (IEEE Cat. No.03CH37440)</span><span>, 2003</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Synchrotron light sources based on Energy Recovery Linacs (ERLs) show promise to deliver X-ray be...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Synchrotron light sources based on Energy Recovery Linacs (ERLs) show promise to deliver X-ray beams with both brilliance and X-ray pulse duration far superior to the values that can be achieved with storage ring technology. Cornell University, in collaboration with Jefferson Laboratory, has proposed the construction of a prototype ERL. This 100MeV, 100mA CW superconducting electron accelerator will be used to study and resolve the many accelerator physics and technology issues of this type of machine. These studies are essential before ERLs can be confidently proposed for large-scale applications such as synchrotron light sources. Key issues include the generation of high average current, high brightness electron beams; acceleration and transport of these beams while preserving their brightness; adequate damping of higher order modes (HOMs) to assure beam stability; removal of large amounts of HOM power from the cryogenic environment; stable RF control of cavities operating at very high external Q; reduction of beam losses to very low levels; and the development of precision non-intercepting diagnostics to allow beam setup, control and characterization. Our prototype design allows us to address these and other issues over a broad range of parameter space. This design, along with recent progress on understanding these issues, will be presented.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="c202d790f62e63321a45964f184a0643" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":50029712,"asset_id":29586662,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/50029712/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="29586662"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="29586662"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 29586662; 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In the injector, a bunched 100 mA, 500 keV beam of a DC gun will be compressed in a normal-conducting copper cavity and subsequently accelerated by five superconducting 2-cell cavities to an energy of 5.5 MeV. We present an overview of the cryomodule design along with the status of the 2-cell HOM-free cavity, the twininput coupler and the ferrite HOM dampers.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="dbc9115674fcc44313722caa25948170" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":50029688,"asset_id":29586648,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/50029688/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="29586648"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="29586648"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 29586648; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=29586648]").text(description); $(".js-view-count[data-work-id=29586648]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 29586648; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='29586648']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-a9bf3a2bc8c89fa2a77156577594264ee8a0f214d74241bc0fcd3f69f8d107ac.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (true){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "dbc9115674fcc44313722caa25948170" } } $('.js-work-strip[data-work-id=29586648]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":29586648,"title":"An overview of the cryomodule for the Cornell ERL injector","internal_url":"https://www.academia.edu/29586648/An_overview_of_the_cryomodule_for_the_Cornell_ERL_injector","owner_id":5103660,"coauthors_can_edit":true,"owner":{"id":5103660,"first_name":"Buz","middle_initials":null,"last_name":"Barstow","page_name":"BuzBarstow","domain_name":"hms-harvard","created_at":"2013-08-11T09:43:28.377-07:00","display_name":"Buz Barstow","url":"https://hms-harvard.academia.edu/BuzBarstow"},"attachments":[{"id":50029688,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/50029688/thumbnails/1.jpg","file_name":"mopkf076.pdf","download_url":"https://www.academia.edu/attachments/50029688/download_file","bulk_download_file_name":"An_overview_of_the_cryomodule_for_the_Co.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/50029688/mopkf076-libre.pdf?1478003279=\u0026response-content-disposition=attachment%3B+filename%3DAn_overview_of_the_cryomodule_for_the_Co.pdf\u0026Expires=1740485057\u0026Signature=RYFwjBQW4~kflvyvud2QMPDokhfnTCaln92zCnVHXpZKOFUPg5sNS~9he97yE4qyc-8T6CKoJERLh99AipVIrDScarXiB8syF1CM3ghxz7stYutA8bAZKLhrCq1fIy6lBFvh36mXG44W6e3VuDsHDc7tH0wC4Xqxh-KO~vxccROeRwbi3X9UP8f33mwG82MwePq2iuM-RcFj605r-gnUbRerz98giA2hhj1kk1m~yyUI-LmyDnS9NXFKluvc4HjB7lNnntsbO8S2ck30dJp0dXkEEkAMb-UNYM50Wk0QheQHgvsBlfVAtXzVZMuDWPbffaXhiv~iaCkYCKRsl3axww__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="29586646"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" rel="nofollow" href="https://www.academia.edu/29586646/Phase_Behavior_of_Water_inside_Protein_Crystals"><img alt="Research paper thumbnail of Phase Behavior of Water inside Protein Crystals" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" rel="nofollow" href="https://www.academia.edu/29586646/Phase_Behavior_of_Water_inside_Protein_Crystals">Phase Behavior of Water inside Protein Crystals</a></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="29586646"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="29586646"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 29586646; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=29586646]").text(description); $(".js-view-count[data-work-id=29586646]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 29586646; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='29586646']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-a9bf3a2bc8c89fa2a77156577594264ee8a0f214d74241bc0fcd3f69f8d107ac.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (false){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "-1" } } $('.js-work-strip[data-work-id=29586646]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":29586646,"title":"Phase Behavior of Water inside Protein Crystals","internal_url":"https://www.academia.edu/29586646/Phase_Behavior_of_Water_inside_Protein_Crystals","owner_id":5103660,"coauthors_can_edit":true,"owner":{"id":5103660,"first_name":"Buz","middle_initials":null,"last_name":"Barstow","page_name":"BuzBarstow","domain_name":"hms-harvard","created_at":"2013-08-11T09:43:28.377-07:00","display_name":"Buz Barstow","url":"https://hms-harvard.academia.edu/BuzBarstow"},"attachments":[]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="4218110"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/4218110/A_synthetic_system_links_FeFe_hydrogenases_to_essential_E_coli_sulfur_metabolism"><img alt="Research paper thumbnail of A synthetic system links FeFe-hydrogenases to essential E. coli sulfur metabolism" class="work-thumbnail" src="https://attachments.academia-assets.com/49981908/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/4218110/A_synthetic_system_links_FeFe_hydrogenases_to_essential_E_coli_sulfur_metabolism">A synthetic system links FeFe-hydrogenases to essential E. coli sulfur metabolism</a></div><div class="wp-workCard_item"><span>Journal of Biological Engineering</span><span>, 2011</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Background FeFe-hydrogenases are the most active class of H2-producing enzymes known in nature an...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Background FeFe-hydrogenases are the most active class of H2-producing enzymes known in nature and may have important applications in clean H2 energy production. Many potential uses are currently complicated by a crucial weakness: the active sites of all known FeFe-hydrogenases are irreversibly inactivated by O2. Results We have developed a synthetic metabolic pathway in E. coli that links FeFe-hydrogenase activity to the production of the essential amino acid cysteine. Our design includes a complementary host strain whose endogenous redox pool is insulated from the synthetic metabolic pathway. Host viability on a selective medium requires hydrogenase expression, and moderate O2 levels eliminate growth. This pathway forms the basis for a genetic selection for O2 tolerance. Genetically selected hydrogenases did not show improved stability in O2 and in many cases had lost H2 production activity. The isolated mutations cluster significantly on charged surface residues, suggesting the evolution of binding surfaces that may accelerate hydrogenase electron transfer. Conclusions Rational design can optimize a fully heterologous three-component pathway to provide an essential metabolic flux while remaining insulated from the endogenous redox pool. We have developed a number of convenient in vivo assays to aid in the engineering of synthetic H2 metabolism. Our results also indicate a H2-independent redox activity in three different FeFe-hydrogenases, with implications for the future directed evolution of H2-activating catalysts.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="98e84c0b7f688ce64eaf91dbbeb3830d" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":49981908,"asset_id":4218110,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/49981908/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="4218110"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="4218110"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 4218110; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=4218110]").text(description); $(".js-view-count[data-work-id=4218110]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 4218110; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='4218110']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-a9bf3a2bc8c89fa2a77156577594264ee8a0f214d74241bc0fcd3f69f8d107ac.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (true){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "98e84c0b7f688ce64eaf91dbbeb3830d" } } $('.js-work-strip[data-work-id=4218110]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":4218110,"title":"A synthetic system links FeFe-hydrogenases to essential E. coli sulfur metabolism","internal_url":"https://www.academia.edu/4218110/A_synthetic_system_links_FeFe_hydrogenases_to_essential_E_coli_sulfur_metabolism","owner_id":5103660,"coauthors_can_edit":true,"owner":{"id":5103660,"first_name":"Buz","middle_initials":null,"last_name":"Barstow","page_name":"BuzBarstow","domain_name":"hms-harvard","created_at":"2013-08-11T09:43:28.377-07:00","display_name":"Buz Barstow","url":"https://hms-harvard.academia.edu/BuzBarstow"},"attachments":[{"id":49981908,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/49981908/thumbnails/1.jpg","file_name":"A_synthetic_system_links_FeFe-hydrogenas20161030-12892-16991n1.pdf","download_url":"https://www.academia.edu/attachments/49981908/download_file","bulk_download_file_name":"A_synthetic_system_links_FeFe_hydrogenas.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/49981908/A_synthetic_system_links_FeFe-hydrogenas20161030-12892-16991n1-libre.pdf?1477838932=\u0026response-content-disposition=attachment%3B+filename%3DA_synthetic_system_links_FeFe_hydrogenas.pdf\u0026Expires=1740485057\u0026Signature=Uyw4WWLCfmtwucL5mqw7J-cfQgQEzV6CyRQamiAEGvC5HeVyzBGLX4m8JrDRIkvfV4gPaY6EKI9On45Xh4FBfou07bjO~jSTDNNNLrkmwgQW8Rb6eSttF2FeCmaLdD~UrhdUIUSpjd~ukHhU2xf0BKB7D4NHWc1XJsWC-qkj5e-hRmFVspMilxZVFo2OAvC4UvHi3G7ZpJ9l4u6x453OI9Mjs80DxWa97GByFoNK5UHcBxSf6QvpidIeiWH~9rY7J2M7vJTCdLEIWdxuTECUrCMrgKj3L8rmt473fh9MqrTH8DjMqWxSkx~TzBKYbFhMeXn7w36giWJUGbleunw08w__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="4218105"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/4218105/Evidence_for_liquid_water_during_the_high_density_to_low_density_amorphous_ice_transition"><img alt="Research paper thumbnail of Evidence for liquid water during the high-density to low-density amorphous ice transition" class="work-thumbnail" src="https://attachments.academia-assets.com/31706690/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/4218105/Evidence_for_liquid_water_during_the_high_density_to_low_density_amorphous_ice_transition">Evidence for liquid water during the high-density to low-density amorphous ice transition</a></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Polymorphism of water has been extensively studied, but controversy still exists over the phase t...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Polymorphism of water has been extensively studied, but controversy still exists over the phase transition between high-density amorphous (HDA) and low-density amorphous (LDA) ice. We report the phase behavior of HDA ice inside high-pressure cryocooled protein crystals. Using X-ray diffraction, we demonstrate that the intermediate states in the temperature range from 80 to 170 K can be reconstructed as a linear combination of HDA and LDA ice, suggesting a first-order transition. We found evidence for a liquid state of water during the ice transition based on the protein crystallographic data. These observations open the possibility that the HDA ice induced by high-pressure cryocooling is a genuine glassy form of high-density liquid.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="50f649d16d401d5c2bb3ae0536395f8f" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":31706690,"asset_id":4218105,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/31706690/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="4218105"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="4218105"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 4218105; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=4218105]").text(description); $(".js-view-count[data-work-id=4218105]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 4218105; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='4218105']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-a9bf3a2bc8c89fa2a77156577594264ee8a0f214d74241bc0fcd3f69f8d107ac.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (true){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="4218104"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/4218104/Alteration_of_citrine_structure_by_hydrostatic_pressure_explains_the_accompanying_spectral_shift"><img alt="Research paper thumbnail of Alteration of citrine structure by hydrostatic pressure explains the accompanying spectral shift" class="work-thumbnail" src="https://attachments.academia-assets.com/31706689/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/4218104/Alteration_of_citrine_structure_by_hydrostatic_pressure_explains_the_accompanying_spectral_shift">Alteration of citrine structure by hydrostatic pressure explains the accompanying spectral shift</a></div><div class="wp-workCard_item"><span>Proceedings of The National Academy of Sciences</span><span>, 2008</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">A protein molecule is an intricate system whose function is highly sensitive to small external pe...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">A protein molecule is an intricate system whose function is highly sensitive to small external perturbations. However, no examples that correlate protein function with progressive subangstrom structural perturbations have thus far been presented. To elucidate this relationship, we have investigated a fluorescent protein, citrine, as a model system under high-pressure perturbation. The protein has been compressed to produce deformations of its chromophore by applying a high-pressure cryocooling technique. A closely spaced series of x-ray crystallographic structures reveals that the chromophore undergoes a progressive deformation of up to 0.8 脜 at an applied pressure of 500 MPa. It is experimentally demonstrated that the structural motion is directly correlated with the progressive fluorescence shift of citrine from yellow to green under these conditions. This protein is therefore highly sensitive to subangstrom deformations and its function must be understood at the subangstrom level. These results have significant implications for protein function prediction and biomolecule design and engineering, because they suggest methods to tune protein function by modification of the protein scaffold.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="6be6a564fae2618950e7b789715c6894" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":31706689,"asset_id":4218104,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/31706689/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="4218104"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="4218104"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 4218104; 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="4218103"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/4218103/Structural_and_Thermodynamic_Characterization_of_T4_Lysozyme_Mutants_and_the_Contribution_of_Internal_Cavities_to_Pressure_Denaturation"><img alt="Research paper thumbnail of Structural and Thermodynamic Characterization of T4 Lysozyme Mutants and the Contribution of Internal Cavities to Pressure Denaturation" class="work-thumbnail" src="https://attachments.academia-assets.com/31706692/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/4218103/Structural_and_Thermodynamic_Characterization_of_T4_Lysozyme_Mutants_and_the_Contribution_of_Internal_Cavities_to_Pressure_Denaturation">Structural and Thermodynamic Characterization of T4 Lysozyme Mutants and the Contribution of Internal Cavities to Pressure Denaturation</a></div><div class="wp-workCard_item"><span>Biophysical Journal</span><span>, 2009</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">The characterization of non-native states stabilized under a variety of conditions is important t...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">The characterization of non-native states stabilized under a variety of conditions is important towards understanding how proteins fold into their biologically functional, native structures (2). It is widely believed that the dominant driving force in protein folding is the hydrophobic effect and that denaturation can be described as the transfer of hydrophobic residues to water. Although the hydrophobic compound transfer model (3-6) largely succeeds in explaining the thermodynamic stability of proteins as a function of temperature, it does not explain denaturation with pressure . In particular, this model fails to explain the magnitude and pressure dependence of the volume difference between the native and denatured states. Recent simulation studies and experimental work suggest that this failure is due to fundamental differences between the temperature-and pressure-denatured states of a protein (1,. These studies suggest that unlike thermally and chemically denatured states, the pressuredenatured state is one in which water penetration into the protein is favorable, and that a significant contribution to the volume reduction with pressure is the hydration of internal cavities or packing defects.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="dd7c3cf6022852b80647125416cfa9fc" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":31706692,"asset_id":4218103,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/31706692/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="4218103"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="4218103"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 4218103; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=4218103]").text(description); $(".js-view-count[data-work-id=4218103]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 4218103; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='4218103']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-a9bf3a2bc8c89fa2a77156577594264ee8a0f214d74241bc0fcd3f69f8d107ac.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (true){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "dd7c3cf6022852b80647125416cfa9fc" } } $('.js-work-strip[data-work-id=4218103]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":4218103,"title":"Structural and Thermodynamic Characterization of T4 Lysozyme Mutants and the Contribution of Internal Cavities to Pressure Denaturation","internal_url":"https://www.academia.edu/4218103/Structural_and_Thermodynamic_Characterization_of_T4_Lysozyme_Mutants_and_the_Contribution_of_Internal_Cavities_to_Pressure_Denaturation","owner_id":5103660,"coauthors_can_edit":true,"owner":{"id":5103660,"first_name":"Buz","middle_initials":null,"last_name":"Barstow","page_name":"BuzBarstow","domain_name":"hms-harvard","created_at":"2013-08-11T09:43:28.377-07:00","display_name":"Buz Barstow","url":"https://hms-harvard.academia.edu/BuzBarstow"},"attachments":[{"id":31706692,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/31706692/thumbnails/1.jpg","file_name":"240_Ando_author_version.pdf","download_url":"https://www.academia.edu/attachments/31706692/download_file","bulk_download_file_name":"Structural_and_Thermodynamic_Characteriz.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/31706692/240_Ando_author_version-libre.pdf?1392373390=\u0026response-content-disposition=attachment%3B+filename%3DStructural_and_Thermodynamic_Characteriz.pdf\u0026Expires=1740485057\u0026Signature=Lzlb9R6x~sWacA7Cf0IWfpaBXHWT3CCP-bdru2tqTbM~67CCHexjWSAHUdxzL70B9yMyNBE66r9xn2Im9pJ06oY-ssMSfL8K-mjgZOjb8NWDNDkG76WrP9byotKOw9tqBcz4KHTq98Qt7iYsomv21clhRQIPMc-SGigTRjlMbc91DI66-ujazYLv~omCYtLwV9ANO-jekfa~ib9o1ICviGsGoe~qNuK-scy9LLzEpxhyOpopT-oYOl6No5lw8HaLVHRVwLlf7XO54nGS2UnGJ-8EWp6mbwzRK0-rB90KvaOsEEsrT-u1cu-dqoo7SnZSqi6kayzDYnAboqjte~QNjg__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="4218102"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/4218102/Evidence_for_liquid_water_during_the_high_density_to_low_density_amorphous_ice_transition"><img alt="Research paper thumbnail of Evidence for liquid water during the high-density to low-density amorphous ice transition" class="work-thumbnail" src="https://attachments.academia-assets.com/49981909/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/4218102/Evidence_for_liquid_water_during_the_high_density_to_low_density_amorphous_ice_transition">Evidence for liquid water during the high-density to low-density amorphous ice transition</a></div><div class="wp-workCard_item"><span>Proceedings of The National Academy of Sciences</span><span>, 2009</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Polymorphism of water has been extensively studied, but controversy still exists over the phase t...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Polymorphism of water has been extensively studied, but controversy still exists over the phase transition between high-density amorphous (HDA) and low-density amorphous (LDA) ice. We report the phase behavior of HDA ice inside high-pressure cryocooled protein crystals. Using X-ray diffraction, we demonstrate that the intermediate states in the temperature range from 80 to 170 K can be reconstructed as a linear combination of HDA and LDA ice, suggesting a first-order transition. We found evidence for a liquid state of water during the ice transition based on the protein crystallographic data. These observations open the possibility that the HDA ice induced by high-pressure cryocooling is a genuine glassy form of high-density liquid.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="ff0d8bdc84b4bcf0ba23acae10357ec3" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":49981909,"asset_id":4218102,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/49981909/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="4218102"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="4218102"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 4218102; 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="4218101"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/4218101/Alteration_of_citrine_structure_by_hydrostatic_pressure_explains_the_accompanying_spectral_shift"><img alt="Research paper thumbnail of Alteration of citrine structure by hydrostatic pressure explains the accompanying spectral shift" class="work-thumbnail" src="https://attachments.academia-assets.com/49981898/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/4218101/Alteration_of_citrine_structure_by_hydrostatic_pressure_explains_the_accompanying_spectral_shift">Alteration of citrine structure by hydrostatic pressure explains the accompanying spectral shift</a></div><div class="wp-workCard_item"><span>Proceedings of The National Academy of Sciences</span><span>, 2008</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">A protein molecule is an intricate system whose function is highly sensitive to small external pe...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">A protein molecule is an intricate system whose function is highly sensitive to small external perturbations. However, no examples that correlate protein function with progressive subangstrom structural perturbations have thus far been presented. To elucidate this relationship, we have investigated a fluorescent protein, citrine, as a model system under high-pressure perturbation. The protein has been compressed to produce deformations of its chromophore by applying a high-pressure cryocooling technique. A closely spaced series of x-ray crystallographic structures reveals that the chromophore undergoes a progressive deformation of up to 0.8 脜 at an applied pressure of 500 MPa. It is experimentally demonstrated that the structural motion is directly correlated with the progressive fluorescence shift of citrine from yellow to green under these conditions. This protein is therefore highly sensitive to subangstrom deformations and its function must be understood at the subangstrom level. These results have significant implications for protein function prediction and biomolecule design and engineering, because they suggest methods to tune protein function by modification of the protein scaffold.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="cc6ed6290ee7f41a22d3025e24a6280b" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":49981898,"asset_id":4218101,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/49981898/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="4218101"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="4218101"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 4218101; 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="4218100"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/4218100/Coupling_of_Pressure_Induced_Structural_Shifts_to_Spectral_Changes_in_a_Yellow_Fluorescent_Protein"><img alt="Research paper thumbnail of Coupling of Pressure-Induced Structural Shifts to Spectral Changes in a Yellow Fluorescent Protein" class="work-thumbnail" src="https://attachments.academia-assets.com/49981912/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/4218100/Coupling_of_Pressure_Induced_Structural_Shifts_to_Spectral_Changes_in_a_Yellow_Fluorescent_Protein">Coupling of Pressure-Induced Structural Shifts to Spectral Changes in a Yellow Fluorescent Protein</a></div><div class="wp-workCard_item"><span>Biophysical Journal</span><span>, 2009</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">X-ray diffraction analysis of pressure-induced structural changes in the Aequorea yellow fluoresc...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">X-ray diffraction analysis of pressure-induced structural changes in the Aequorea yellow fluorescent protein Citrine reveals the structural basis for the continuous fluorescence peak shift from yellow to green that is observed on pressurization. This fluorescence peak shift is caused by a reorientation of the two elements of the Citrine chromophore. This study describes the structural linkages in Citrine that are responsible for the local reorientation of the chromophore. The deformation of the Citrine chromophore is actuated by the differential motion of two clusters of atoms that compose the b-barrel scaffold of the molecule, resulting in a slight bending of the b-barrel. The high-pressure structures also show a perturbation of the hydrogen bonding network that stabilizes the excited state of the Citrine chromophore. The perturbation of this network is implicated in the reduction of fluorescence intensity of Citrine. The blue-shift of the Citrine fluorescence spectrum resulting from the bending of the b-barrel provides structural insight into the transient blue-shifting of isolated yellow fluorescent protein molecules under ambient conditions and suggests mechanisms to alter the time-dependent behavior of Citrine under ambient conditions.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="e0ee727f839b6fd784385486c3f08fbc" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":49981912,"asset_id":4218100,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/49981912/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="4218100"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="4218100"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 4218100; 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</script> <div class="js-work-strip profile--work_container" data-work-id="29586666"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/29586666/First_studies_for_a_low_temperature_higher_order_mode_absorber_for_the_Cornell_ERL_prototype"><img alt="Research paper thumbnail of First studies for a low temperature higher-order-mode absorber for the Cornell ERL prototype" class="work-thumbnail" src="https://attachments.academia-assets.com/50029709/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/29586666/First_studies_for_a_low_temperature_higher_order_mode_absorber_for_the_Cornell_ERL_prototype">First studies for a low temperature higher-order-mode absorber for the Cornell ERL prototype</a></div><div class="wp-workCard_item"><span>Proceedings of the 2003 Bipolar/BiCMOS Circuits and Technology Meeting (IEEE Cat. No.03CH37440)</span><span>, 2003</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Cornell University, in collaboration with Jefferson Laboratory, has proposed the construction of ...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Cornell University, in collaboration with Jefferson Laboratory, has proposed the construction of a prototype energyrecovery linac (ERL) to study the energy recovery concept with high current, low emittance beams . The beam with a current of up to 100 mA will excite significant higher-order-mode (HOM) power in the superconducting (s.c.) RF cavities with frequencies up to 100 GHz. Strong damping of the HOMs is essential for beam stability and to reduce the HOM losses to a few hundred Watts per meter. To achieve this demanding goal we plan to place RF absorbing material in the beam tubes between the cavities in the linac. However, this will require operating the HOM absorbers at temperatures below 80 K to simplify the thermal transition to the cavities at 2 K with low static losses to 2 K. One possible material candidate is ferrite, as it is used at room temperature in the HOM absorbers in the s.c. CESR cavities. In this paper we present experiments performed to study the RF absorption properties of ferrite at cryogenic temperatures in the frequency range from 1 GHz to 15 GHz. First results are shown and the resulting HOM damping is evaluated and discussed. 0-7803-7739-9</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="72253f4a7f60f3b5767a61b45afe4af1" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":50029709,"asset_id":29586666,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/50029709/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="29586666"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="29586666"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 29586666; 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="29586664"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/29586664/Overview_of_the_cornell_ERL_injector_cryomodule"><img alt="Research paper thumbnail of Overview of the cornell ERL injector cryomodule" class="work-thumbnail" src="https://attachments.academia-assets.com/50029704/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/29586664/Overview_of_the_cornell_ERL_injector_cryomodule">Overview of the cornell ERL injector cryomodule</a></div><div class="wp-workCard_item"><span>Proceedings of the 2003 Bipolar/BiCMOS Circuits and Technology Meeting (IEEE Cat. No.03CH37440)</span><span>, 2003</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">The Laboratory for Elementary-Particle Physics, Cornell University, in collaboration with Jeffers...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">The Laboratory for Elementary-Particle Physics, Cornell University, in collaboration with Jefferson Lab is exploring the potential of a Synchrotron Radiation User Facility based on a multi-GeV, low emittance, Energy-Recovery Linac (ERL) with a 100 mA CW beam[1]. The ERL injector will accelerate bunches from the electron source from 0.5 MeV to 5 MeV with minimal emittance growth. The injector and main linac of the ERL will be based on superconducting RF technology to provide CW operation. There will be one cryomodule with five 1300 MHz 2-cell cavities, each providing one MV of acceleration, corresponding to an accelerating field of about 4.3 MV/m in CW operation. Besides standard features such as an integrated helium vessel and mechanical tuner, each cavity has two input couplers, symmetrically placed on the beam pipe to cancel kicks due to coupler fields. For a 100 mA maximum injected beam current, each coupler must deliver 50 kW of beam power leading to a Qext of 4.6 x10 4 for matched beam loading conditions. Antenna-and loop-based HOM couplers can disturb beam emittance through kicks. We plan to avoid the use of such couplers. Following the strategy for B-factory SRF cavities, the beam pipe aperture has been enlarged on one side to propagate all higher order modes out to symmetric ferrite beam pipe loads. These are positioned outside the helium vessel and cooled to liquid nitrogen temperature. Ferrite properties at 77 K have been measured and the corresponding damping evaluated. To explore the full capabilities of the injector, energy gains up to 3 MV per cavity will be considered at lower beam currents. For this flexibility, the input coupling needs to be adjustable by a factor of 9.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="ca962725e5e59f39df479dfe53898b6a" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":50029704,"asset_id":29586664,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/50029704/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="29586664"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="29586664"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 29586664; 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="29586662"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/29586662/The_Cornell_ERL_prototype_project"><img alt="Research paper thumbnail of The Cornell ERL prototype project" class="work-thumbnail" src="https://attachments.academia-assets.com/50029712/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/29586662/The_Cornell_ERL_prototype_project">The Cornell ERL prototype project</a></div><div class="wp-workCard_item"><span>Proceedings of the 2003 Bipolar/BiCMOS Circuits and Technology Meeting (IEEE Cat. No.03CH37440)</span><span>, 2003</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Synchrotron light sources based on Energy Recovery Linacs (ERLs) show promise to deliver X-ray be...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Synchrotron light sources based on Energy Recovery Linacs (ERLs) show promise to deliver X-ray beams with both brilliance and X-ray pulse duration far superior to the values that can be achieved with storage ring technology. Cornell University, in collaboration with Jefferson Laboratory, has proposed the construction of a prototype ERL. This 100MeV, 100mA CW superconducting electron accelerator will be used to study and resolve the many accelerator physics and technology issues of this type of machine. These studies are essential before ERLs can be confidently proposed for large-scale applications such as synchrotron light sources. Key issues include the generation of high average current, high brightness electron beams; acceleration and transport of these beams while preserving their brightness; adequate damping of higher order modes (HOMs) to assure beam stability; removal of large amounts of HOM power from the cryogenic environment; stable RF control of cavities operating at very high external Q; reduction of beam losses to very low levels; and the development of precision non-intercepting diagnostics to allow beam setup, control and characterization. Our prototype design allows us to address these and other issues over a broad range of parameter space. 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dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "-1" } } $('.js-work-strip[data-work-id=29586650]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":29586650,"title":"Engineering a light source for the future","internal_url":"https://www.academia.edu/29586650/Engineering_a_light_source_for_the_future","owner_id":5103660,"coauthors_can_edit":true,"owner":{"id":5103660,"first_name":"Buz","middle_initials":null,"last_name":"Barstow","page_name":"BuzBarstow","domain_name":"hms-harvard","created_at":"2013-08-11T09:43:28.377-07:00","display_name":"Buz Barstow","url":"https://hms-harvard.academia.edu/BuzBarstow"},"attachments":[]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="29586648"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/29586648/An_overview_of_the_cryomodule_for_the_Cornell_ERL_injector"><img alt="Research paper thumbnail of An overview of the cryomodule for the Cornell ERL injector" class="work-thumbnail" src="https://attachments.academia-assets.com/50029688/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/29586648/An_overview_of_the_cryomodule_for_the_Cornell_ERL_injector">An overview of the cryomodule for the Cornell ERL injector</a></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">The first stage of the Cornell ERL project will be a 100 MeV, 100 mA (CW) prototype machine to st...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">The first stage of the Cornell ERL project will be a 100 MeV, 100 mA (CW) prototype machine to study the energy recovery concept with high current, low emittance beams. In the injector, a bunched 100 mA, 500 keV beam of a DC gun will be compressed in a normal-conducting copper cavity and subsequently accelerated by five superconducting 2-cell cavities to an energy of 5.5 MeV. We present an overview of the cryomodule design along with the status of the 2-cell HOM-free cavity, the twininput coupler and the ferrite HOM dampers.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="dbc9115674fcc44313722caa25948170" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":50029688,"asset_id":29586648,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/50029688/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="29586648"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="29586648"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 29586648; 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="29586646"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" rel="nofollow" href="https://www.academia.edu/29586646/Phase_Behavior_of_Water_inside_Protein_Crystals"><img alt="Research paper thumbnail of Phase Behavior of Water inside Protein Crystals" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" rel="nofollow" href="https://www.academia.edu/29586646/Phase_Behavior_of_Water_inside_Protein_Crystals">Phase Behavior of Water inside Protein Crystals</a></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="29586646"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="29586646"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 29586646; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=29586646]").text(description); $(".js-view-count[data-work-id=29586646]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 29586646; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='29586646']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-a9bf3a2bc8c89fa2a77156577594264ee8a0f214d74241bc0fcd3f69f8d107ac.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (false){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "-1" } } $('.js-work-strip[data-work-id=29586646]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":29586646,"title":"Phase Behavior of Water inside Protein Crystals","internal_url":"https://www.academia.edu/29586646/Phase_Behavior_of_Water_inside_Protein_Crystals","owner_id":5103660,"coauthors_can_edit":true,"owner":{"id":5103660,"first_name":"Buz","middle_initials":null,"last_name":"Barstow","page_name":"BuzBarstow","domain_name":"hms-harvard","created_at":"2013-08-11T09:43:28.377-07:00","display_name":"Buz Barstow","url":"https://hms-harvard.academia.edu/BuzBarstow"},"attachments":[]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="4218110"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/4218110/A_synthetic_system_links_FeFe_hydrogenases_to_essential_E_coli_sulfur_metabolism"><img alt="Research paper thumbnail of A synthetic system links FeFe-hydrogenases to essential E. coli sulfur metabolism" class="work-thumbnail" src="https://attachments.academia-assets.com/49981908/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/4218110/A_synthetic_system_links_FeFe_hydrogenases_to_essential_E_coli_sulfur_metabolism">A synthetic system links FeFe-hydrogenases to essential E. coli sulfur metabolism</a></div><div class="wp-workCard_item"><span>Journal of Biological Engineering</span><span>, 2011</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Background FeFe-hydrogenases are the most active class of H2-producing enzymes known in nature an...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Background FeFe-hydrogenases are the most active class of H2-producing enzymes known in nature and may have important applications in clean H2 energy production. Many potential uses are currently complicated by a crucial weakness: the active sites of all known FeFe-hydrogenases are irreversibly inactivated by O2. Results We have developed a synthetic metabolic pathway in E. coli that links FeFe-hydrogenase activity to the production of the essential amino acid cysteine. Our design includes a complementary host strain whose endogenous redox pool is insulated from the synthetic metabolic pathway. Host viability on a selective medium requires hydrogenase expression, and moderate O2 levels eliminate growth. This pathway forms the basis for a genetic selection for O2 tolerance. Genetically selected hydrogenases did not show improved stability in O2 and in many cases had lost H2 production activity. The isolated mutations cluster significantly on charged surface residues, suggesting the evolution of binding surfaces that may accelerate hydrogenase electron transfer. Conclusions Rational design can optimize a fully heterologous three-component pathway to provide an essential metabolic flux while remaining insulated from the endogenous redox pool. We have developed a number of convenient in vivo assays to aid in the engineering of synthetic H2 metabolism. Our results also indicate a H2-independent redox activity in three different FeFe-hydrogenases, with implications for the future directed evolution of H2-activating catalysts.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="98e84c0b7f688ce64eaf91dbbeb3830d" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":49981908,"asset_id":4218110,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/49981908/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="4218110"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="4218110"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 4218110; 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="4218105"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/4218105/Evidence_for_liquid_water_during_the_high_density_to_low_density_amorphous_ice_transition"><img alt="Research paper thumbnail of Evidence for liquid water during the high-density to low-density amorphous ice transition" class="work-thumbnail" src="https://attachments.academia-assets.com/31706690/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/4218105/Evidence_for_liquid_water_during_the_high_density_to_low_density_amorphous_ice_transition">Evidence for liquid water during the high-density to low-density amorphous ice transition</a></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Polymorphism of water has been extensively studied, but controversy still exists over the phase t...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Polymorphism of water has been extensively studied, but controversy still exists over the phase transition between high-density amorphous (HDA) and low-density amorphous (LDA) ice. We report the phase behavior of HDA ice inside high-pressure cryocooled protein crystals. Using X-ray diffraction, we demonstrate that the intermediate states in the temperature range from 80 to 170 K can be reconstructed as a linear combination of HDA and LDA ice, suggesting a first-order transition. We found evidence for a liquid state of water during the ice transition based on the protein crystallographic data. These observations open the possibility that the HDA ice induced by high-pressure cryocooling is a genuine glassy form of high-density liquid.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="50f649d16d401d5c2bb3ae0536395f8f" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":31706690,"asset_id":4218105,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/31706690/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="4218105"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="4218105"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 4218105; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=4218105]").text(description); $(".js-view-count[data-work-id=4218105]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 4218105; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='4218105']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-a9bf3a2bc8c89fa2a77156577594264ee8a0f214d74241bc0fcd3f69f8d107ac.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (true){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "50f649d16d401d5c2bb3ae0536395f8f" } } $('.js-work-strip[data-work-id=4218105]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":4218105,"title":"Evidence for liquid water during the high-density to low-density amorphous ice transition","internal_url":"https://www.academia.edu/4218105/Evidence_for_liquid_water_during_the_high_density_to_low_density_amorphous_ice_transition","owner_id":5103660,"coauthors_can_edit":true,"owner":{"id":5103660,"first_name":"Buz","middle_initials":null,"last_name":"Barstow","page_name":"BuzBarstow","domain_name":"hms-harvard","created_at":"2013-08-11T09:43:28.377-07:00","display_name":"Buz Barstow","url":"https://hms-harvard.academia.edu/BuzBarstow"},"attachments":[{"id":31706690,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/31706690/thumbnails/1.jpg","file_name":"245_Kim.pdf","download_url":"https://www.academia.edu/attachments/31706690/download_file","bulk_download_file_name":"Evidence_for_liquid_water_during_the_hig.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/31706690/245_Kim-libre.pdf?1392326382=\u0026response-content-disposition=attachment%3B+filename%3DEvidence_for_liquid_water_during_the_hig.pdf\u0026Expires=1740485057\u0026Signature=UlOjdxCDkHE-gzsTb8bcuGezKlPfnfrmfciM9u1WsypNBLvb7GnPs1djlcGdt67EJ~r3G6BEmGGQfIJYf3fyWuarOSbmqY8eukcOkcEIKDVSrpqwEIQMBNWVKbSFDt7-szcP2Eb6Wlwy30YyLl0wBV0lVo6K6PV7dsnPFb2kqvGvSKtgP8~fbFt3huj~n7T1gZWZZuv~gPuKelDCWGiMULLGk5QTC2SHxru54FV~01s4zdgL-1S2l0mz5UdcWcRwCwly~trYdkwzhdbJFKbJ4HA~MpTyRdAYXhe6KaskQT5XLUPofWAD7PtkEAbIr9Bg~KGRaIzrIQ~vdRjKgcHGjw__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="4218104"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/4218104/Alteration_of_citrine_structure_by_hydrostatic_pressure_explains_the_accompanying_spectral_shift"><img alt="Research paper thumbnail of Alteration of citrine structure by hydrostatic pressure explains the accompanying spectral shift" class="work-thumbnail" src="https://attachments.academia-assets.com/31706689/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/4218104/Alteration_of_citrine_structure_by_hydrostatic_pressure_explains_the_accompanying_spectral_shift">Alteration of citrine structure by hydrostatic pressure explains the accompanying spectral shift</a></div><div class="wp-workCard_item"><span>Proceedings of The National Academy of Sciences</span><span>, 2008</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">A protein molecule is an intricate system whose function is highly sensitive to small external pe...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">A protein molecule is an intricate system whose function is highly sensitive to small external perturbations. However, no examples that correlate protein function with progressive subangstrom structural perturbations have thus far been presented. To elucidate this relationship, we have investigated a fluorescent protein, citrine, as a model system under high-pressure perturbation. The protein has been compressed to produce deformations of its chromophore by applying a high-pressure cryocooling technique. A closely spaced series of x-ray crystallographic structures reveals that the chromophore undergoes a progressive deformation of up to 0.8 脜 at an applied pressure of 500 MPa. It is experimentally demonstrated that the structural motion is directly correlated with the progressive fluorescence shift of citrine from yellow to green under these conditions. This protein is therefore highly sensitive to subangstrom deformations and its function must be understood at the subangstrom level. These results have significant implications for protein function prediction and biomolecule design and engineering, because they suggest methods to tune protein function by modification of the protein scaffold.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="6be6a564fae2618950e7b789715c6894" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":31706689,"asset_id":4218104,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/31706689/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="4218104"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="4218104"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 4218104; 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="4218103"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/4218103/Structural_and_Thermodynamic_Characterization_of_T4_Lysozyme_Mutants_and_the_Contribution_of_Internal_Cavities_to_Pressure_Denaturation"><img alt="Research paper thumbnail of Structural and Thermodynamic Characterization of T4 Lysozyme Mutants and the Contribution of Internal Cavities to Pressure Denaturation" class="work-thumbnail" src="https://attachments.academia-assets.com/31706692/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/4218103/Structural_and_Thermodynamic_Characterization_of_T4_Lysozyme_Mutants_and_the_Contribution_of_Internal_Cavities_to_Pressure_Denaturation">Structural and Thermodynamic Characterization of T4 Lysozyme Mutants and the Contribution of Internal Cavities to Pressure Denaturation</a></div><div class="wp-workCard_item"><span>Biophysical Journal</span><span>, 2009</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">The characterization of non-native states stabilized under a variety of conditions is important t...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">The characterization of non-native states stabilized under a variety of conditions is important towards understanding how proteins fold into their biologically functional, native structures (2). It is widely believed that the dominant driving force in protein folding is the hydrophobic effect and that denaturation can be described as the transfer of hydrophobic residues to water. Although the hydrophobic compound transfer model (3-6) largely succeeds in explaining the thermodynamic stability of proteins as a function of temperature, it does not explain denaturation with pressure . In particular, this model fails to explain the magnitude and pressure dependence of the volume difference between the native and denatured states. Recent simulation studies and experimental work suggest that this failure is due to fundamental differences between the temperature-and pressure-denatured states of a protein (1,. These studies suggest that unlike thermally and chemically denatured states, the pressuredenatured state is one in which water penetration into the protein is favorable, and that a significant contribution to the volume reduction with pressure is the hydration of internal cavities or packing defects.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="dd7c3cf6022852b80647125416cfa9fc" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":31706692,"asset_id":4218103,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/31706692/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="4218103"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="4218103"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 4218103; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=4218103]").text(description); $(".js-view-count[data-work-id=4218103]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 4218103; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='4218103']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-a9bf3a2bc8c89fa2a77156577594264ee8a0f214d74241bc0fcd3f69f8d107ac.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (true){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "dd7c3cf6022852b80647125416cfa9fc" } } $('.js-work-strip[data-work-id=4218103]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":4218103,"title":"Structural and Thermodynamic Characterization of T4 Lysozyme Mutants and the Contribution of Internal Cavities to Pressure Denaturation","internal_url":"https://www.academia.edu/4218103/Structural_and_Thermodynamic_Characterization_of_T4_Lysozyme_Mutants_and_the_Contribution_of_Internal_Cavities_to_Pressure_Denaturation","owner_id":5103660,"coauthors_can_edit":true,"owner":{"id":5103660,"first_name":"Buz","middle_initials":null,"last_name":"Barstow","page_name":"BuzBarstow","domain_name":"hms-harvard","created_at":"2013-08-11T09:43:28.377-07:00","display_name":"Buz Barstow","url":"https://hms-harvard.academia.edu/BuzBarstow"},"attachments":[{"id":31706692,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/31706692/thumbnails/1.jpg","file_name":"240_Ando_author_version.pdf","download_url":"https://www.academia.edu/attachments/31706692/download_file","bulk_download_file_name":"Structural_and_Thermodynamic_Characteriz.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/31706692/240_Ando_author_version-libre.pdf?1392373390=\u0026response-content-disposition=attachment%3B+filename%3DStructural_and_Thermodynamic_Characteriz.pdf\u0026Expires=1740485057\u0026Signature=Lzlb9R6x~sWacA7Cf0IWfpaBXHWT3CCP-bdru2tqTbM~67CCHexjWSAHUdxzL70B9yMyNBE66r9xn2Im9pJ06oY-ssMSfL8K-mjgZOjb8NWDNDkG76WrP9byotKOw9tqBcz4KHTq98Qt7iYsomv21clhRQIPMc-SGigTRjlMbc91DI66-ujazYLv~omCYtLwV9ANO-jekfa~ib9o1ICviGsGoe~qNuK-scy9LLzEpxhyOpopT-oYOl6No5lw8HaLVHRVwLlf7XO54nGS2UnGJ-8EWp6mbwzRK0-rB90KvaOsEEsrT-u1cu-dqoo7SnZSqi6kayzDYnAboqjte~QNjg__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="4218102"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/4218102/Evidence_for_liquid_water_during_the_high_density_to_low_density_amorphous_ice_transition"><img alt="Research paper thumbnail of Evidence for liquid water during the high-density to low-density amorphous ice transition" class="work-thumbnail" src="https://attachments.academia-assets.com/49981909/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/4218102/Evidence_for_liquid_water_during_the_high_density_to_low_density_amorphous_ice_transition">Evidence for liquid water during the high-density to low-density amorphous ice transition</a></div><div class="wp-workCard_item"><span>Proceedings of The National Academy of Sciences</span><span>, 2009</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Polymorphism of water has been extensively studied, but controversy still exists over the phase t...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Polymorphism of water has been extensively studied, but controversy still exists over the phase transition between high-density amorphous (HDA) and low-density amorphous (LDA) ice. We report the phase behavior of HDA ice inside high-pressure cryocooled protein crystals. Using X-ray diffraction, we demonstrate that the intermediate states in the temperature range from 80 to 170 K can be reconstructed as a linear combination of HDA and LDA ice, suggesting a first-order transition. We found evidence for a liquid state of water during the ice transition based on the protein crystallographic data. These observations open the possibility that the HDA ice induced by high-pressure cryocooling is a genuine glassy form of high-density liquid.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="ff0d8bdc84b4bcf0ba23acae10357ec3" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":49981909,"asset_id":4218102,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/49981909/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="4218102"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="4218102"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 4218102; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=4218102]").text(description); $(".js-view-count[data-work-id=4218102]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 4218102; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='4218102']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-a9bf3a2bc8c89fa2a77156577594264ee8a0f214d74241bc0fcd3f69f8d107ac.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (true){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "ff0d8bdc84b4bcf0ba23acae10357ec3" } } $('.js-work-strip[data-work-id=4218102]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":4218102,"title":"Evidence for liquid water during the high-density to low-density amorphous ice transition","internal_url":"https://www.academia.edu/4218102/Evidence_for_liquid_water_during_the_high_density_to_low_density_amorphous_ice_transition","owner_id":5103660,"coauthors_can_edit":true,"owner":{"id":5103660,"first_name":"Buz","middle_initials":null,"last_name":"Barstow","page_name":"BuzBarstow","domain_name":"hms-harvard","created_at":"2013-08-11T09:43:28.377-07:00","display_name":"Buz Barstow","url":"https://hms-harvard.academia.edu/BuzBarstow"},"attachments":[{"id":49981909,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/49981909/thumbnails/1.jpg","file_name":"Evidence_for_liquid_water_during_the_hig20161030-12892-1u3dir1.pdf","download_url":"https://www.academia.edu/attachments/49981909/download_file","bulk_download_file_name":"Evidence_for_liquid_water_during_the_hig.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/49981909/Evidence_for_liquid_water_during_the_hig20161030-12892-1u3dir1-libre.pdf?1477838925=\u0026response-content-disposition=attachment%3B+filename%3DEvidence_for_liquid_water_during_the_hig.pdf\u0026Expires=1740485057\u0026Signature=Q7gYq~aNqvv-x-Syt2tyhOeE473EYH2HH1cWySbNT0QSg9tIdyDDZRHuatvS3b520wk0IyEz1DPZsluwMtM9DTR0kUHnfFyBgKgkFmhdQiAIVhgio0-hpSeJnuoq517z9efovb1KNhxR9xyD3VFkQM6U7liLqk2n4XmeuAt1XTPlhwS2XNNrhO65FLepbGFm-GhDur5hI9OxkEYAj2moicbJgflCizaLen8svmLpskLGlG9FCdPM4A48eAQ9R3EIYa-JxiUU2X~kb17nGauLgyfsUFncmOK6L2JONCYCsv5rodsn4VXdT96Ype3cYqmSN9K3I6aJYkuk7vNbtMEqAA__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="4218101"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/4218101/Alteration_of_citrine_structure_by_hydrostatic_pressure_explains_the_accompanying_spectral_shift"><img alt="Research paper thumbnail of Alteration of citrine structure by hydrostatic pressure explains the accompanying spectral shift" class="work-thumbnail" src="https://attachments.academia-assets.com/49981898/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/4218101/Alteration_of_citrine_structure_by_hydrostatic_pressure_explains_the_accompanying_spectral_shift">Alteration of citrine structure by hydrostatic pressure explains the accompanying spectral shift</a></div><div class="wp-workCard_item"><span>Proceedings of The National Academy of Sciences</span><span>, 2008</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">A protein molecule is an intricate system whose function is highly sensitive to small external pe...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">A protein molecule is an intricate system whose function is highly sensitive to small external perturbations. However, no examples that correlate protein function with progressive subangstrom structural perturbations have thus far been presented. To elucidate this relationship, we have investigated a fluorescent protein, citrine, as a model system under high-pressure perturbation. The protein has been compressed to produce deformations of its chromophore by applying a high-pressure cryocooling technique. A closely spaced series of x-ray crystallographic structures reveals that the chromophore undergoes a progressive deformation of up to 0.8 脜 at an applied pressure of 500 MPa. It is experimentally demonstrated that the structural motion is directly correlated with the progressive fluorescence shift of citrine from yellow to green under these conditions. This protein is therefore highly sensitive to subangstrom deformations and its function must be understood at the subangstrom level. These results have significant implications for protein function prediction and biomolecule design and engineering, because they suggest methods to tune protein function by modification of the protein scaffold.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="cc6ed6290ee7f41a22d3025e24a6280b" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":49981898,"asset_id":4218101,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/49981898/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="4218101"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="4218101"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 4218101; 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="4218100"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/4218100/Coupling_of_Pressure_Induced_Structural_Shifts_to_Spectral_Changes_in_a_Yellow_Fluorescent_Protein"><img alt="Research paper thumbnail of Coupling of Pressure-Induced Structural Shifts to Spectral Changes in a Yellow Fluorescent Protein" class="work-thumbnail" src="https://attachments.academia-assets.com/49981912/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/4218100/Coupling_of_Pressure_Induced_Structural_Shifts_to_Spectral_Changes_in_a_Yellow_Fluorescent_Protein">Coupling of Pressure-Induced Structural Shifts to Spectral Changes in a Yellow Fluorescent Protein</a></div><div class="wp-workCard_item"><span>Biophysical Journal</span><span>, 2009</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">X-ray diffraction analysis of pressure-induced structural changes in the Aequorea yellow fluoresc...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">X-ray diffraction analysis of pressure-induced structural changes in the Aequorea yellow fluorescent protein Citrine reveals the structural basis for the continuous fluorescence peak shift from yellow to green that is observed on pressurization. This fluorescence peak shift is caused by a reorientation of the two elements of the Citrine chromophore. This study describes the structural linkages in Citrine that are responsible for the local reorientation of the chromophore. The deformation of the Citrine chromophore is actuated by the differential motion of two clusters of atoms that compose the b-barrel scaffold of the molecule, resulting in a slight bending of the b-barrel. The high-pressure structures also show a perturbation of the hydrogen bonding network that stabilizes the excited state of the Citrine chromophore. The perturbation of this network is implicated in the reduction of fluorescence intensity of Citrine. The blue-shift of the Citrine fluorescence spectrum resulting from the bending of the b-barrel provides structural insight into the transient blue-shifting of isolated yellow fluorescent protein molecules under ambient conditions and suggests mechanisms to alter the time-dependent behavior of Citrine under ambient conditions.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="e0ee727f839b6fd784385486c3f08fbc" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":49981912,"asset_id":4218100,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/49981912/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="4218100"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="4218100"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 4218100; 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