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data-dom-id="Pill-react-component-1183635a-80f0-47aa-bcaf-22716632f244"></div> <div id="Pill-react-component-1183635a-80f0-47aa-bcaf-22716632f244"></div> </a></div></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 Doletha Szebenyi</h3></div><div class="js-work-strip profile--work_container" data-work-id="71703801"><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/71703801/A_high_pressure_macromolecular_crystallography_capability_developed_at_CHESS"><img alt="Research paper thumbnail of A high-pressure macromolecular crystallography capability developed at CHESS" class="work-thumbnail" src="https://attachments.academia-assets.com/80936977/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/71703801/A_high_pressure_macromolecular_crystallography_capability_developed_at_CHESS">A high-pressure macromolecular crystallography capability developed at CHESS</a></div><div class="wp-workCard_item"><span>Acta Crystallographica Section A Foundations and Advances</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="05dc9a93ecf6709038f8579eb014468e" 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href="https://www.academia.edu/58804552/Endogenous_Synthesis_of_Erythritol_a_Novel_Biomarker_of_Weight_Gain_P15_016_19_"><img alt="Research paper thumbnail of Endogenous Synthesis of Erythritol, a Novel Biomarker of Weight Gain (P15-016-19)" class="work-thumbnail" src="https://attachments.academia-assets.com/73038781/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/58804552/Endogenous_Synthesis_of_Erythritol_a_Novel_Biomarker_of_Weight_Gain_P15_016_19_">Endogenous Synthesis of Erythritol, a Novel Biomarker of Weight Gain (P15-016-19)</a></div><div class="wp-workCard_item"><span>Current Developments in Nutrition</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Objectives Serum erythritol is associated with central adiposity gain in young adults. Erythritol...</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">Objectives Serum erythritol is associated with central adiposity gain in young adults. Erythritol, a 4-carbon polyol, is synthesized endogenously from erythrose through the pentose phosphate pathway. We have identified two enzymes which catalyze this reaction: alcohol dehydrogenase 1 (ADH1) and sorbitol dehydrogenase (SORD). Interestingly, ADH1 isoforms ADH1B1 and ADH1C2 catalyze NADPH-dependent synthesis of erythritol in vitro, but ADH1B1 does not. In A549 cells, siRNA knockdown of SORD levels to less than 15% of control levels reduced erythritol by 50%. A549 cells also have low levels of ADH1 expression. This indicates that other enzymes may be capable of endogenous erythritol production. Based on its high degree of homology to ADH1, we hypothesize that ADH4 also catalyzes erythritol synthesis. The objective of this study was to further elucidate the mechanism of erythritol synthesis by: determining key differences between the active site of ADH1B2 compared to ADH1B1 and SORD, and...</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="480505fdc2b906640e79df9b891cb0f3" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":73038781,"asset_id":58804552,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/73038781/download_file?st=MTczMjcyMTY1OSw4LjIyMi4yMDguMTQ2&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="58804552"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="58804552"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 58804552; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=58804552]").text(description); $(".js-view-count[data-work-id=58804552]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 58804552; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='58804552']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 58804552, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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: "480505fdc2b906640e79df9b891cb0f3" } } $('.js-work-strip[data-work-id=58804552]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":58804552,"title":"Endogenous Synthesis of Erythritol, a Novel Biomarker of Weight Gain (P15-016-19)","translated_title":"","metadata":{"abstract":"Objectives Serum erythritol is associated with central adiposity gain in young adults. Erythritol, a 4-carbon polyol, is synthesized endogenously from erythrose through the pentose phosphate pathway. We have identified two enzymes which catalyze this reaction: alcohol dehydrogenase 1 (ADH1) and sorbitol dehydrogenase (SORD). Interestingly, ADH1 isoforms ADH1B1 and ADH1C2 catalyze NADPH-dependent synthesis of erythritol in vitro, but ADH1B1 does not. In A549 cells, siRNA knockdown of SORD levels to less than 15% of control levels reduced erythritol by 50%. A549 cells also have low levels of ADH1 expression. This indicates that other enzymes may be capable of endogenous erythritol production. Based on its high degree of homology to ADH1, we hypothesize that ADH4 also catalyzes erythritol synthesis. 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It is fairly common that a visually well formed crystal diffracts poorly to a resolution that is too low to be suitable for structure determination. Dehydration has proven to be an effective post-crystallization treatment for improving crystal diffraction quality. Several dehydration methods have been developed, but no single one of them is suitable for all crystals. Here, a new convenient and effective dehydration method is reported that makes use of a dehydrating solution that will not dry out in air for several hours. Using this dehydration method, the resolution ofArchaeoglobus fulgidusCas5a crystals has been increased from 3.2 to 1.95 Å and the resolution ofEscherichia coliLptA crystals has been increased from…</span></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="58804543"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="58804543"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 58804543; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=58804543]").text(description); $(".js-view-count[data-work-id=58804543]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 58804543; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='58804543']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 58804543, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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" } } $('.js-work-strip[data-work-id=58804543]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":58804543,"title":"Improving diffraction resolution using a new dehydration method","translated_title":"","metadata":{"abstract":"The production of high-quality crystals is one of the major obstacles in determining the three-dimensional structure of macromolecules by X-ray crystallography. 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Using this dehydration method, the resolution ofArchaeoglobus fulgidusCas5a crystals has been increased from 3.2 to 1.95 Å and the resolution ofEscherichia coliLptA crystals has been increased from…","publisher":"International Union of Crystallography (IUCr)","publication_date":{"day":null,"month":null,"year":2016,"errors":{}},"publication_name":"Acta Crystallographica Section F Structural Biology Communications"},"translated_abstract":"The production of high-quality crystals is one of the major obstacles in determining the three-dimensional structure of macromolecules by X-ray crystallography. It is fairly common that a visually well formed crystal diffracts poorly to a resolution that is too low to be suitable for structure determination. Dehydration has proven to be an effective post-crystallization treatment for improving crystal diffraction quality. Several dehydration methods have been developed, but no single one of them is suitable for all crystals. Here, a new convenient and effective dehydration method is reported that makes use of a dehydrating solution that will not dry out in air for several hours. Using this dehydration method, the resolution ofArchaeoglobus fulgidusCas5a crystals has been increased from 3.2 to 1.95 Å and the resolution ofEscherichia coliLptA crystals has been increased from…","internal_url":"https://www.academia.edu/58804543/Improving_diffraction_resolution_using_a_new_dehydration_method","translated_internal_url":"","created_at":"2021-10-18T05:55:24.252-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":33002650,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Improving_diffraction_resolution_using_a_new_dehydration_method","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":33002650,"first_name":"Doletha","middle_initials":null,"last_name":"Szebenyi","page_name":"DolethaSzebenyi","domain_name":"cornell","created_at":"2015-07-12T07:19:02.115-07:00","display_name":"Doletha Szebenyi","url":"https://cornell.academia.edu/DolethaSzebenyi"},"attachments":[],"research_interests":[{"id":12597,"name":"Crystallization","url":"https://www.academia.edu/Documents/in/Crystallization"},{"id":33441,"name":"Macromolecular X-Ray Crystallography","url":"https://www.academia.edu/Documents/in/Macromolecular_X-Ray_Crystallography"},{"id":83128,"name":"Escherichia coli","url":"https://www.academia.edu/Documents/in/Escherichia_coli"},{"id":346274,"name":"Dehydration","url":"https://www.academia.edu/Documents/in/Dehydration"},{"id":653665,"name":"Protein Conformation","url":"https://www.academia.edu/Documents/in/Protein_Conformation"},{"id":3663861,"name":"Archaeoglobus fulgidus","url":"https://www.academia.edu/Documents/in/Archaeoglobus_fulgidus"}],"urls":[]}, 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="58804540"><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/58804540/A_visible_light_excited_fluorescence_method_for_imaging_protein_crystals_without_added_dyes"><img alt="Research paper thumbnail of A visible-light-excited fluorescence method for imaging protein crystals without added dyes" 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" href="https://www.academia.edu/58804540/A_visible_light_excited_fluorescence_method_for_imaging_protein_crystals_without_added_dyes">A visible-light-excited fluorescence method for imaging protein crystals without added dyes</a></div><div class="wp-workCard_item"><span>Journal of Applied Crystallography</span><span>, 2016</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Fluorescence microscopy methods have seen an increase in popularity in recent years for detecting...</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">Fluorescence microscopy methods have seen an increase in popularity in recent years for detecting protein crystals in screening trays. The fluorescence-based crystal detection methods have thus far relied on intrinsic UV-inducible tryptophan fluorescence, nonlinear optics or fluorescence in the visible light range dependent on crystals soaked with fluorescent dyes. In this paper data are presented on a novel visible-light-inducible autofluorescence arising from protein crystals as a result of general stabilization of conjugated double-bond systems and increased charge delocalization due to crystal packing. The visible-light-inducible autofluorescence serves as a complementary method to bright-field microscopy in beamline applications where accurate crystal centering about the rotation axis is essential. Owing to temperature-dependent chromophore stabilization, protein crystals exhibit tenfold higher fluorescence intensity at cryogenic temperatures, making the method ideal for experi...</span></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="58804540"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="58804540"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 58804540; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=58804540]").text(description); $(".js-view-count[data-work-id=58804540]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 58804540; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='58804540']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 58804540, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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" } } $('.js-work-strip[data-work-id=58804540]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":58804540,"title":"A visible-light-excited fluorescence method for imaging protein crystals without added dyes","translated_title":"","metadata":{"abstract":"Fluorescence microscopy methods have seen an increase in popularity in recent years for detecting protein crystals in screening trays. The fluorescence-based crystal detection methods have thus far relied on intrinsic UV-inducible tryptophan fluorescence, nonlinear optics or fluorescence in the visible light range dependent on crystals soaked with fluorescent dyes. In this paper data are presented on a novel visible-light-inducible autofluorescence arising from protein crystals as a result of general stabilization of conjugated double-bond systems and increased charge delocalization due to crystal packing. The visible-light-inducible autofluorescence serves as a complementary method to bright-field microscopy in beamline applications where accurate crystal centering about the rotation axis is essential. Owing to temperature-dependent chromophore stabilization, protein crystals exhibit tenfold higher fluorescence intensity at cryogenic temperatures, making the method ideal for experi...","publisher":"International Union of Crystallography (IUCr)","publication_date":{"day":null,"month":null,"year":2016,"errors":{}},"publication_name":"Journal of Applied Crystallography"},"translated_abstract":"Fluorescence microscopy methods have seen an increase in popularity in recent years for detecting protein crystals in screening trays. The fluorescence-based crystal detection methods have thus far relied on intrinsic UV-inducible tryptophan fluorescence, nonlinear optics or fluorescence in the visible light range dependent on crystals soaked with fluorescent dyes. In this paper data are presented on a novel visible-light-inducible autofluorescence arising from protein crystals as a result of general stabilization of conjugated double-bond systems and increased charge delocalization due to crystal packing. The visible-light-inducible autofluorescence serves as a complementary method to bright-field microscopy in beamline applications where accurate crystal centering about the rotation axis is essential. Owing to temperature-dependent chromophore stabilization, protein crystals exhibit tenfold higher fluorescence intensity at cryogenic temperatures, making the method ideal for experi...","internal_url":"https://www.academia.edu/58804540/A_visible_light_excited_fluorescence_method_for_imaging_protein_crystals_without_added_dyes","translated_internal_url":"","created_at":"2021-10-18T05:55:24.141-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":33002650,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"A_visible_light_excited_fluorescence_method_for_imaging_protein_crystals_without_added_dyes","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":33002650,"first_name":"Doletha","middle_initials":null,"last_name":"Szebenyi","page_name":"DolethaSzebenyi","domain_name":"cornell","created_at":"2015-07-12T07:19:02.115-07:00","display_name":"Doletha Szebenyi","url":"https://cornell.academia.edu/DolethaSzebenyi"},"attachments":[],"research_interests":[{"id":48,"name":"Engineering","url":"https://www.academia.edu/Documents/in/Engineering"},{"id":80414,"name":"Mathematical Sciences","url":"https://www.academia.edu/Documents/in/Mathematical_Sciences"},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences"},{"id":734874,"name":"Applied Crystallography","url":"https://www.academia.edu/Documents/in/Applied_Crystallography"}],"urls":[]}, 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="58804538"><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/58804538/Reduction_of_lattice_disorder_in_protein_crystals_by_high_pressure_cryocooling"><img alt="Research paper thumbnail of Reduction of lattice disorder in protein crystals by high-pressure cryocooling" 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" href="https://www.academia.edu/58804538/Reduction_of_lattice_disorder_in_protein_crystals_by_high_pressure_cryocooling">Reduction of lattice disorder in protein crystals by high-pressure cryocooling</a></div><div class="wp-workCard_item"><span>Journal of Applied Crystallography</span><span>, 2016</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">High-pressure cryocooling (HPC) has been developed as a technique for reducing the damage that fr...</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">High-pressure cryocooling (HPC) has been developed as a technique for reducing the damage that frequently occurs when macromolecular crystals are cryocooled at ambient pressure. Crystals are typically pressurized at around 200 MPa and then cooled to liquid nitrogen temperature under pressure; this process reduces the need for penetrating cryoprotectants, as well as the damage due to cryocooling, but does not improve the diffraction quality of the as-grown crystals. Here it is reported that HPC using a pressure above 300 MPa can reduce lattice disorder, in the form of high mosaicity and/or nonmerohedral twinning, in crystals of three different proteins, namely human glutaminase C, the GTP pyrophosphokinase YjbM and the uncharacterized protein lpg1496. Pressure lower than 250 MPa does not induce this transformation, even with a prolonged pressurization time. These results indicate that HPC at elevated pressures can be a useful tool for improving crystal packing and hence the quality o...</span></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="58804538"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="58804538"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 58804538; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=58804538]").text(description); $(".js-view-count[data-work-id=58804538]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 58804538; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='58804538']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 58804538, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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" } } $('.js-work-strip[data-work-id=58804538]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":58804538,"title":"Reduction of lattice disorder in protein crystals by high-pressure cryocooling","translated_title":"","metadata":{"abstract":"High-pressure cryocooling (HPC) has been developed as a technique for reducing the damage that frequently occurs when macromolecular crystals are cryocooled at ambient pressure. Crystals are typically pressurized at around 200 MPa and then cooled to liquid nitrogen temperature under pressure; this process reduces the need for penetrating cryoprotectants, as well as the damage due to cryocooling, but does not improve the diffraction quality of the as-grown crystals. Here it is reported that HPC using a pressure above 300 MPa can reduce lattice disorder, in the form of high mosaicity and/or nonmerohedral twinning, in crystals of three different proteins, namely human glutaminase C, the GTP pyrophosphokinase YjbM and the uncharacterized protein lpg1496. Pressure lower than 250 MPa does not induce this transformation, even with a prolonged pressurization time. These results indicate that HPC at elevated pressures can be a useful tool for improving crystal packing and hence the quality o...","publisher":"International Union of Crystallography (IUCr)","publication_date":{"day":null,"month":null,"year":2016,"errors":{}},"publication_name":"Journal of Applied Crystallography"},"translated_abstract":"High-pressure cryocooling (HPC) has been developed as a technique for reducing the damage that frequently occurs when macromolecular crystals are cryocooled at ambient pressure. Crystals are typically pressurized at around 200 MPa and then cooled to liquid nitrogen temperature under pressure; this process reduces the need for penetrating cryoprotectants, as well as the damage due to cryocooling, but does not improve the diffraction quality of the as-grown crystals. Here it is reported that HPC using a pressure above 300 MPa can reduce lattice disorder, in the form of high mosaicity and/or nonmerohedral twinning, in crystals of three different proteins, namely human glutaminase C, the GTP pyrophosphokinase YjbM and the uncharacterized protein lpg1496. Pressure lower than 250 MPa does not induce this transformation, even with a prolonged pressurization time. These results indicate that HPC at elevated pressures can be a useful tool for improving crystal packing and hence the quality o...","internal_url":"https://www.academia.edu/58804538/Reduction_of_lattice_disorder_in_protein_crystals_by_high_pressure_cryocooling","translated_internal_url":"","created_at":"2021-10-18T05:55:24.033-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":33002650,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Reduction_of_lattice_disorder_in_protein_crystals_by_high_pressure_cryocooling","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":33002650,"first_name":"Doletha","middle_initials":null,"last_name":"Szebenyi","page_name":"DolethaSzebenyi","domain_name":"cornell","created_at":"2015-07-12T07:19:02.115-07:00","display_name":"Doletha Szebenyi","url":"https://cornell.academia.edu/DolethaSzebenyi"},"attachments":[],"research_interests":[{"id":48,"name":"Engineering","url":"https://www.academia.edu/Documents/in/Engineering"},{"id":80414,"name":"Mathematical Sciences","url":"https://www.academia.edu/Documents/in/Mathematical_Sciences"},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences"},{"id":734874,"name":"Applied Crystallography","url":"https://www.academia.edu/Documents/in/Applied_Crystallography"}],"urls":[]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="58804536"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/58804536/Quantitative_analysis_of_Laue_diffraction_patterns_recorded_with_a_120_ps_exposure_from_an_X_ray_undulator"><img alt="Research paper thumbnail of Quantitative analysis of Laue diffraction patterns recorded with a 120 ps exposure from an X-ray undulator" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/58804536/Quantitative_analysis_of_Laue_diffraction_patterns_recorded_with_a_120_ps_exposure_from_an_X_ray_undulator">Quantitative analysis of Laue diffraction patterns recorded with a 120 ps exposure from an X-ray undulator</a></div><div class="wp-workCard_item"><span>Journal of Applied Crystallography</span><span>, 1992</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="58804536"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="58804536"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 58804536; 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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="58804532"><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/58804532/Lack_of_Catalytic_Activity_of_a_Murine_mRNA_Cytoplasmic_Serine_Hydroxymethyltransferase_Splice_Variant_Evidence_against_Alternative_Splicing_as_a_Regulatory_Mechanism_"><img alt="Research paper thumbnail of Lack of Catalytic Activity of a Murine mRNA Cytoplasmic Serine Hydroxymethyltransferase Splice Variant: Evidence against Alternative Splicing as a Regulatory Mechanism †" 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" href="https://www.academia.edu/58804532/Lack_of_Catalytic_Activity_of_a_Murine_mRNA_Cytoplasmic_Serine_Hydroxymethyltransferase_Splice_Variant_Evidence_against_Alternative_Splicing_as_a_Regulatory_Mechanism_">Lack of Catalytic Activity of a Murine mRNA Cytoplasmic Serine Hydroxymethyltransferase Splice Variant: Evidence against Alternative Splicing as a Regulatory Mechanism †</a></div><div class="wp-workCard_item"><span>Biochemistry Usa</span><span>, May 1, 2001</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Mammalian serine hydroxymethyltransferase (SHMT) is a tetrameric, pyridoxal phosphate-dependent e...</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">Mammalian serine hydroxymethyltransferase (SHMT) is a tetrameric, pyridoxal phosphate-dependent enzyme that catalyzes the reversible interconversion of serine and tetrahydrofolate to glycine and methylenetetrahydrofolate. This reaction generates single-carbon units for purine, thymidine, and methionine biosynthesis. Cytoplasmic SHMT (cSHMT) has been postulated to channel one-carbon substituted folates to various folate-dependent enzymes, and alternative splicing of the cSHMT transcript may be a mechanism that enables specific protein-protein interactions. The cytoplasmic isozyme is expressed from species-specific and tissue-specific alternatively spliced transcripts that encode proteins with modified carboxy-terminal domains, while the mitochondrial isozyme is expressed from a single transcript. While the full-length mouse and human cSHMT proteins are 91% identical, their alternatively spliced transcripts differ. The murine cSHMT gene is expressed as two transcripts. One transcript encodes a full-length 55 kDa active enzyme (cSHMT), while the other transcript encodes a 35 kDa protein (McSHMTtr). The McSHMTtr protein present in mouse liver and kidney does not bind 5-formyltetrahydrofolate, nor does it oligomerize with the full-length cSHMT enzyme. While recombinant cSHMT-glutathione S-transferase fusion proteins form tetramers and are catalytically active, McSHMTtr-glutathione S-transferase fusion proteins are catalytically inactive, do not form heterotetramers, and do not bind pyridoxal phosphate. Analysis of the murine cSHMT crystal structure indicates that the active site lysine that normally binds pyridoxal phosphate in the cSHMT protein is exposed to solvent in the McSHMTtr protein, preventing stable formation of a Schiff base with pyridoxal phosphate. Modeling studies suggest that the human cSHMT proteins expressed from alternatively spliced transcripts are inactive as well. Therefore, channeling mechanisms enabling specific protein-protein interactions of active enzymes are not based on cSHMT alternative splicing.</span></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="58804532"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="58804532"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 58804532; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=58804532]").text(description); $(".js-view-count[data-work-id=58804532]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 58804532; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='58804532']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 58804532, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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" } } $('.js-work-strip[data-work-id=58804532]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":58804532,"title":"Lack of Catalytic Activity of a Murine mRNA Cytoplasmic Serine Hydroxymethyltransferase Splice Variant: Evidence against Alternative Splicing as a Regulatory Mechanism †","translated_title":"","metadata":{"abstract":"Mammalian serine hydroxymethyltransferase (SHMT) is a tetrameric, pyridoxal phosphate-dependent enzyme that catalyzes the reversible interconversion of serine and tetrahydrofolate to glycine and methylenetetrahydrofolate. This reaction generates single-carbon units for purine, thymidine, and methionine biosynthesis. Cytoplasmic SHMT (cSHMT) has been postulated to channel one-carbon substituted folates to various folate-dependent enzymes, and alternative splicing of the cSHMT transcript may be a mechanism that enables specific protein-protein interactions. The cytoplasmic isozyme is expressed from species-specific and tissue-specific alternatively spliced transcripts that encode proteins with modified carboxy-terminal domains, while the mitochondrial isozyme is expressed from a single transcript. While the full-length mouse and human cSHMT proteins are 91% identical, their alternatively spliced transcripts differ. The murine cSHMT gene is expressed as two transcripts. One transcript encodes a full-length 55 kDa active enzyme (cSHMT), while the other transcript encodes a 35 kDa protein (McSHMTtr). The McSHMTtr protein present in mouse liver and kidney does not bind 5-formyltetrahydrofolate, nor does it oligomerize with the full-length cSHMT enzyme. While recombinant cSHMT-glutathione S-transferase fusion proteins form tetramers and are catalytically active, McSHMTtr-glutathione S-transferase fusion proteins are catalytically inactive, do not form heterotetramers, and do not bind pyridoxal phosphate. Analysis of the murine cSHMT crystal structure indicates that the active site lysine that normally binds pyridoxal phosphate in the cSHMT protein is exposed to solvent in the McSHMTtr protein, preventing stable formation of a Schiff base with pyridoxal phosphate. Modeling studies suggest that the human cSHMT proteins expressed from alternatively spliced transcripts are inactive as well. Therefore, channeling mechanisms enabling specific protein-protein interactions of active enzymes are not based on cSHMT alternative splicing.","publication_date":{"day":1,"month":5,"year":2001,"errors":{}},"publication_name":"Biochemistry Usa"},"translated_abstract":"Mammalian serine hydroxymethyltransferase (SHMT) is a tetrameric, pyridoxal phosphate-dependent enzyme that catalyzes the reversible interconversion of serine and tetrahydrofolate to glycine and methylenetetrahydrofolate. This reaction generates single-carbon units for purine, thymidine, and methionine biosynthesis. Cytoplasmic SHMT (cSHMT) has been postulated to channel one-carbon substituted folates to various folate-dependent enzymes, and alternative splicing of the cSHMT transcript may be a mechanism that enables specific protein-protein interactions. The cytoplasmic isozyme is expressed from species-specific and tissue-specific alternatively spliced transcripts that encode proteins with modified carboxy-terminal domains, while the mitochondrial isozyme is expressed from a single transcript. While the full-length mouse and human cSHMT proteins are 91% identical, their alternatively spliced transcripts differ. The murine cSHMT gene is expressed as two transcripts. One transcript encodes a full-length 55 kDa active enzyme (cSHMT), while the other transcript encodes a 35 kDa protein (McSHMTtr). The McSHMTtr protein present in mouse liver and kidney does not bind 5-formyltetrahydrofolate, nor does it oligomerize with the full-length cSHMT enzyme. While recombinant cSHMT-glutathione S-transferase fusion proteins form tetramers and are catalytically active, McSHMTtr-glutathione S-transferase fusion proteins are catalytically inactive, do not form heterotetramers, and do not bind pyridoxal phosphate. 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In part, this is because SAXS benefits greatly from the sensitivity and throughput that can be achieved at modern high brightness synchrotron sources. However, the critical need for highly monodisperse samples in SAXS analysis can be a challenge, and as such a number of labs have moved to develop in-line Size Exclusion Chromatography (SEC) at the beamline. Real-time SAXS on elution profiles not only improves monodispersity of samples and provides information on possible oligomeric states, but it also offers new modes of data analysis that can take advantage of the inherent concentration profiles underlying elution peaks and distributions of partially resolved species. Efforts to extend the synergy between SEC and SAXS to other biophysical methods are ongoing. The newly commissi...</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="b75fb6374dafd7e11c83cfbbc3c3f64a" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":73038769,"asset_id":58804527,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/73038769/download_file?st=MTczMjcyMTY1OSw4LjIyMi4yMDguMTQ2&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="58804527"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="58804527"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 58804527; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=58804527]").text(description); $(".js-view-count[data-work-id=58804527]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 58804527; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='58804527']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 58804527, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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: "b75fb6374dafd7e11c83cfbbc3c3f64a" } } $('.js-work-strip[data-work-id=58804527]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":58804527,"title":"In-line SEC-SAXS and MALS/DLS/RI for the Analysis of Polydisperse Macromolecules","translated_title":"","metadata":{"abstract":"Small Angle X-ray Scattering (SAXS) is a powerful tool for the structural analysis of biological macromolecules in solution and has seen a surge in popularity amongst structural biologists in the past decade. 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We have determined to 2.0 Å resolution the structure of Aplysia cyclase with ribose-5-phosphate bound covalently at C3′ and with the base exchange substrate (BES), pyridylcarbinol, bound to the active site. In addition, further refinement at 2.4 Å</span></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="58804526"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="58804526"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 58804526; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=58804526]").text(description); $(".js-view-count[data-work-id=58804526]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 58804526; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='58804526']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 58804526, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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" } } $('.js-work-strip[data-work-id=58804526]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":58804526,"title":"ADP-Ribosyl Cyclase","translated_title":"","metadata":{"abstract":"ADP-ribosyl cyclase catalyzes the elimination of nicotinamide from NAD and cyclization to cADPR, a known second messenger in cellular calcium signaling pathways. We have determined to 2.0 Å resolution the structure of Aplysia cyclase with ribose-5-phosphate bound covalently at C3′ and with the base exchange substrate (BES), pyridylcarbinol, bound to the active site. In addition, further refinement at 2.4 Å","publication_date":{"day":null,"month":null,"year":2004,"errors":{}},"publication_name":"Structure"},"translated_abstract":"ADP-ribosyl cyclase catalyzes the elimination of nicotinamide from NAD and cyclization to cADPR, a known second messenger in cellular calcium signaling pathways. We have determined to 2.0 Å resolution the structure of Aplysia cyclase with ribose-5-phosphate bound covalently at C3′ and with the base exchange substrate (BES), pyridylcarbinol, bound to the active site. In addition, further refinement at 2.4 Å","internal_url":"https://www.academia.edu/58804526/ADP_Ribosyl_Cyclase","translated_internal_url":"","created_at":"2021-10-18T05:55:23.218-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":33002650,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"ADP_Ribosyl_Cyclase","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":33002650,"first_name":"Doletha","middle_initials":null,"last_name":"Szebenyi","page_name":"DolethaSzebenyi","domain_name":"cornell","created_at":"2015-07-12T07:19:02.115-07:00","display_name":"Doletha Szebenyi","url":"https://cornell.academia.edu/DolethaSzebenyi"},"attachments":[],"research_interests":[{"id":3614,"name":"Structure","url":"https://www.academia.edu/Documents/in/Structure"},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences"},{"id":140081,"name":"Calcium Signaling","url":"https://www.academia.edu/Documents/in/Calcium_Signaling"},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES"},{"id":354019,"name":"Active site","url":"https://www.academia.edu/Documents/in/Active_site"},{"id":1200088,"name":"Second Messengers","url":"https://www.academia.edu/Documents/in/Second_Messengers"}],"urls":[{"id":13315672,"url":"http://sciencedirect.com/science/article/pii/s0969212604000486"}]}, 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="58804525"><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/58804525/Carbon_Dioxide_Trapped_in_a_%CE%B2_Carbonic_Anhydrase"><img alt="Research paper thumbnail of Carbon Dioxide “Trapped” in a β-Carbonic Anhydrase" 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" href="https://www.academia.edu/58804525/Carbon_Dioxide_Trapped_in_a_%CE%B2_Carbonic_Anhydrase">Carbon Dioxide “Trapped” in a β-Carbonic Anhydrase</a></div><div class="wp-workCard_item"><span>Biochemistry</span><span>, 2015</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Carbonic anhydrases (CAs) are enzymes that catalyze the hydration/dehydration of CO2/HCO3(-) with...</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">Carbonic anhydrases (CAs) are enzymes that catalyze the hydration/dehydration of CO2/HCO3(-) with rates approaching diffusion-controlled limits (kcat/KM ∼ 10(8) M(-1) s(-1)). This family of enzymes has evolved disparate protein folds that all perform the same reaction at near catalytic perfection. Presented here is a structural study of a β-CA (psCA3) expressed in Pseudomonas aeruginosa, in complex with CO2, using pressurized cryo-cooled crystallography. The structure has been refined to 1.6 Å resolution with Rcryst and Rfree values of 17.3 and 19.9%, respectively, and is compared with the α-CA, human CA isoform II (hCA II), the only other CA to have CO2 captured in its active site. Despite the lack of structural similarity between psCA3 and hCA II, the CO2 binding orientation relative to the zinc-bound solvent is identical. In addition, a second CO2 binding site was located at the dimer interface of psCA3. Interestingly, all β-CAs function as dimers or higher-order oligomeric states, and the CO2 bound at the interface may contribute to the allosteric nature of this family of enzymes or may be a convenient alternative binding site as this pocket has been previously shown to be a promiscuous site for a variety of ligands, including bicarbonate, sulfate, and phosphate ions.</span></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="58804525"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="58804525"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 58804525; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=58804525]").text(description); $(".js-view-count[data-work-id=58804525]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 58804525; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='58804525']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 58804525, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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" } } $('.js-work-strip[data-work-id=58804525]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":58804525,"title":"Carbon Dioxide “Trapped” in a β-Carbonic Anhydrase","translated_title":"","metadata":{"abstract":"Carbonic anhydrases (CAs) are enzymes that catalyze the hydration/dehydration of CO2/HCO3(-) with rates approaching diffusion-controlled limits (kcat/KM ∼ 10(8) M(-1) s(-1)). 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Interestingly, all β-CAs function as dimers or higher-order oligomeric states, and the CO2 bound at the interface may contribute to the allosteric nature of this family of enzymes or may be a convenient alternative binding site as this pocket has been previously shown to be a promiscuous site for a variety of ligands, including bicarbonate, sulfate, and phosphate ions.","publisher":"American Chemical Society (ACS)","publication_date":{"day":null,"month":null,"year":2015,"errors":{}},"publication_name":"Biochemistry"},"translated_abstract":"Carbonic anhydrases (CAs) are enzymes that catalyze the hydration/dehydration of CO2/HCO3(-) with rates approaching diffusion-controlled limits (kcat/KM ∼ 10(8) M(-1) s(-1)). This family of enzymes has evolved disparate protein folds that all perform the same reaction at near catalytic perfection. Presented here is a structural study of a β-CA (psCA3) expressed in Pseudomonas aeruginosa, in complex with CO2, using pressurized cryo-cooled crystallography. The structure has been refined to 1.6 Å resolution with Rcryst and Rfree values of 17.3 and 19.9%, respectively, and is compared with the α-CA, human CA isoform II (hCA II), the only other CA to have CO2 captured in its active site. Despite the lack of structural similarity between psCA3 and hCA II, the CO2 binding orientation relative to the zinc-bound solvent is identical. In addition, a second CO2 binding site was located at the dimer interface of psCA3. Interestingly, all β-CAs function as dimers or higher-order oligomeric states, and the CO2 bound at the interface may contribute to the allosteric nature of this family of enzymes or may be a convenient alternative binding site as this pocket has been previously shown to be a promiscuous site for a variety of ligands, including bicarbonate, sulfate, and phosphate ions.","internal_url":"https://www.academia.edu/58804525/Carbon_Dioxide_Trapped_in_a_%CE%B2_Carbonic_Anhydrase","translated_internal_url":"","created_at":"2021-10-18T05:55:23.091-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":33002650,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Carbon_Dioxide_Trapped_in_a_β_Carbonic_Anhydrase","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":33002650,"first_name":"Doletha","middle_initials":null,"last_name":"Szebenyi","page_name":"DolethaSzebenyi","domain_name":"cornell","created_at":"2015-07-12T07:19:02.115-07:00","display_name":"Doletha Szebenyi","url":"https://cornell.academia.edu/DolethaSzebenyi"},"attachments":[],"research_interests":[{"id":145,"name":"Biochemistry","url":"https://www.academia.edu/Documents/in/Biochemistry"},{"id":4594,"name":"Carbon Dioxide","url":"https://www.academia.edu/Documents/in/Carbon_Dioxide"},{"id":33441,"name":"Macromolecular X-Ray Crystallography","url":"https://www.academia.edu/Documents/in/Macromolecular_X-Ray_Crystallography"},{"id":225499,"name":"Pseudomonas aeruginosa","url":"https://www.academia.edu/Documents/in/Pseudomonas_aeruginosa"},{"id":636395,"name":"Pseudomonas Aeruginosa","url":"https://www.academia.edu/Documents/in/Pseudomonas_Aeruginosa-1"},{"id":653665,"name":"Protein Conformation","url":"https://www.academia.edu/Documents/in/Protein_Conformation"},{"id":784076,"name":"Species Specificity","url":"https://www.academia.edu/Documents/in/Species_Specificity"},{"id":956752,"name":"Protein Quaternary Structure","url":"https://www.academia.edu/Documents/in/Protein_Quaternary_Structure"},{"id":990417,"name":"Recombinant Proteins","url":"https://www.academia.edu/Documents/in/Recombinant_Proteins"},{"id":1222191,"name":"Ligands","url":"https://www.academia.edu/Documents/in/Ligands"},{"id":1681026,"name":"Biochemistry and cell biology","url":"https://www.academia.edu/Documents/in/Biochemistry_and_cell_biology"},{"id":3789880,"name":"Medical biochemistry and metabolomics","url":"https://www.academia.edu/Documents/in/Medical_biochemistry_and_metabolomics"}],"urls":[]}, dispatcherData: dispatcherData }); 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Erythritol...</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">Objectives Serum erythritol is associated with central adiposity gain in young adults. Erythritol, a 4-carbon polyol, is synthesized endogenously from erythrose through the pentose phosphate pathway. We have identified two enzymes which catalyze this reaction: alcohol dehydrogenase 1 (ADH1) and sorbitol dehydrogenase (SORD). Interestingly, ADH1 isoforms ADH1B1 and ADH1C2 catalyze NADPH-dependent synthesis of erythritol in vitro, but ADH1B1 does not. In A549 cells, siRNA knockdown of SORD levels to less than 15% of control levels reduced erythritol by 50%. A549 cells also have low levels of ADH1 expression. This indicates that other enzymes may be capable of endogenous erythritol production. Based on its high degree of homology to ADH1, we hypothesize that ADH4 also catalyzes erythritol synthesis. The objective of this study was to further elucidate the mechanism of erythritol synthesis by: determining key differences between the active site of ADH1B2 compared to ADH1B1 and SORD, and...</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="480505fdc2b906640e79df9b891cb0f3" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":73038781,"asset_id":58804552,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/73038781/download_file?st=MTczMjcyMTY1OSw4LjIyMi4yMDguMTQ2&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="58804552"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="58804552"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 58804552; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=58804552]").text(description); $(".js-view-count[data-work-id=58804552]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 58804552; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='58804552']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 58804552, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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: "480505fdc2b906640e79df9b891cb0f3" } } $('.js-work-strip[data-work-id=58804552]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":58804552,"title":"Endogenous Synthesis of Erythritol, a Novel Biomarker of Weight Gain (P15-016-19)","translated_title":"","metadata":{"abstract":"Objectives Serum erythritol is associated with central adiposity gain in young adults. 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The net lies in the hexagonal space group P-6m2 (#187) and there are 10 vertices (or atoms) in the unit cell, including 4 sites of approximately trigonal planar coordination and 6 sites of approximately tetrahedral coordination. All vertices (atoms) in the network sit on special positions in the P-6m2 space group, giving the network high 6-fold symmetry axes parallel to the crystallographic c-axis. The structure has thus been named trigohexagonite in a loose analogy with its hexagonite crystalline homolog, sitting in the hexagonal space group P6/mmm (#191). The Wells point symbol for the trigohexagonite network is given by (7 3)(6 3 8 3) 3 (6.7 2) 3 (3.7 4 .8) 3 where this symbol indicates the quaternary stoichiometry of the network. The Wells point symbol also reveals that the only structural strain present in the network comes from the presence of the 3-gon, cyclopropane-like moieties in it, built on tetrahedral vertices. This structural motif of cyclopropane-like rings has precedent in organic chemistry and it adds character to the overall 6-fold symmetry of the trigohexagonite pattern. Also, the overall network contains rare trimethylenemethane-like clusters of 4 trigonal planar vertices (atoms), bonded together, that constitute the 3connected component of the network. 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It is fairly common that a visually well formed crystal diffracts poorly to a resolution that is too low to be suitable for structure determination. Dehydration has proven to be an effective post-crystallization treatment for improving crystal diffraction quality. Several dehydration methods have been developed, but no single one of them is suitable for all crystals. Here, a new convenient and effective dehydration method is reported that makes use of a dehydrating solution that will not dry out in air for several hours. Using this dehydration method, the resolution ofArchaeoglobus fulgidusCas5a crystals has been increased from 3.2 to 1.95 Å and the resolution ofEscherichia coliLptA crystals has been increased from…</span></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="58804543"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="58804543"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 58804543; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=58804543]").text(description); $(".js-view-count[data-work-id=58804543]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 58804543; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='58804543']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 58804543, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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" } } $('.js-work-strip[data-work-id=58804543]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":58804543,"title":"Improving diffraction resolution using a new dehydration method","translated_title":"","metadata":{"abstract":"The production of high-quality crystals is one of the major obstacles in determining the three-dimensional structure of macromolecules by X-ray crystallography. 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Using this dehydration method, the resolution ofArchaeoglobus fulgidusCas5a crystals has been increased from 3.2 to 1.95 Å and the resolution ofEscherichia coliLptA crystals has been increased from…","publisher":"International Union of Crystallography (IUCr)","publication_date":{"day":null,"month":null,"year":2016,"errors":{}},"publication_name":"Acta Crystallographica Section F Structural Biology Communications"},"translated_abstract":"The production of high-quality crystals is one of the major obstacles in determining the three-dimensional structure of macromolecules by X-ray crystallography. It is fairly common that a visually well formed crystal diffracts poorly to a resolution that is too low to be suitable for structure determination. Dehydration has proven to be an effective post-crystallization treatment for improving crystal diffraction quality. Several dehydration methods have been developed, but no single one of them is suitable for all crystals. Here, a new convenient and effective dehydration method is reported that makes use of a dehydrating solution that will not dry out in air for several hours. Using this dehydration method, the resolution ofArchaeoglobus fulgidusCas5a crystals has been increased from 3.2 to 1.95 Å and the resolution ofEscherichia coliLptA crystals has been increased from…","internal_url":"https://www.academia.edu/58804543/Improving_diffraction_resolution_using_a_new_dehydration_method","translated_internal_url":"","created_at":"2021-10-18T05:55:24.252-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":33002650,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Improving_diffraction_resolution_using_a_new_dehydration_method","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":33002650,"first_name":"Doletha","middle_initials":null,"last_name":"Szebenyi","page_name":"DolethaSzebenyi","domain_name":"cornell","created_at":"2015-07-12T07:19:02.115-07:00","display_name":"Doletha Szebenyi","url":"https://cornell.academia.edu/DolethaSzebenyi"},"attachments":[],"research_interests":[{"id":12597,"name":"Crystallization","url":"https://www.academia.edu/Documents/in/Crystallization"},{"id":33441,"name":"Macromolecular X-Ray Crystallography","url":"https://www.academia.edu/Documents/in/Macromolecular_X-Ray_Crystallography"},{"id":83128,"name":"Escherichia coli","url":"https://www.academia.edu/Documents/in/Escherichia_coli"},{"id":346274,"name":"Dehydration","url":"https://www.academia.edu/Documents/in/Dehydration"},{"id":653665,"name":"Protein Conformation","url":"https://www.academia.edu/Documents/in/Protein_Conformation"},{"id":3663861,"name":"Archaeoglobus fulgidus","url":"https://www.academia.edu/Documents/in/Archaeoglobus_fulgidus"}],"urls":[]}, 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="58804540"><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/58804540/A_visible_light_excited_fluorescence_method_for_imaging_protein_crystals_without_added_dyes"><img alt="Research paper thumbnail of A visible-light-excited fluorescence method for imaging protein crystals without added dyes" 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" href="https://www.academia.edu/58804540/A_visible_light_excited_fluorescence_method_for_imaging_protein_crystals_without_added_dyes">A visible-light-excited fluorescence method for imaging protein crystals without added dyes</a></div><div class="wp-workCard_item"><span>Journal of Applied Crystallography</span><span>, 2016</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Fluorescence microscopy methods have seen an increase in popularity in recent years for detecting...</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">Fluorescence microscopy methods have seen an increase in popularity in recent years for detecting protein crystals in screening trays. The fluorescence-based crystal detection methods have thus far relied on intrinsic UV-inducible tryptophan fluorescence, nonlinear optics or fluorescence in the visible light range dependent on crystals soaked with fluorescent dyes. In this paper data are presented on a novel visible-light-inducible autofluorescence arising from protein crystals as a result of general stabilization of conjugated double-bond systems and increased charge delocalization due to crystal packing. The visible-light-inducible autofluorescence serves as a complementary method to bright-field microscopy in beamline applications where accurate crystal centering about the rotation axis is essential. Owing to temperature-dependent chromophore stabilization, protein crystals exhibit tenfold higher fluorescence intensity at cryogenic temperatures, making the method ideal for experi...</span></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="58804540"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="58804540"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 58804540; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=58804540]").text(description); $(".js-view-count[data-work-id=58804540]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 58804540; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='58804540']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 58804540, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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" } } $('.js-work-strip[data-work-id=58804540]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":58804540,"title":"A visible-light-excited fluorescence method for imaging protein crystals without added dyes","translated_title":"","metadata":{"abstract":"Fluorescence microscopy methods have seen an increase in popularity in recent years for detecting protein crystals in screening trays. The fluorescence-based crystal detection methods have thus far relied on intrinsic UV-inducible tryptophan fluorescence, nonlinear optics or fluorescence in the visible light range dependent on crystals soaked with fluorescent dyes. In this paper data are presented on a novel visible-light-inducible autofluorescence arising from protein crystals as a result of general stabilization of conjugated double-bond systems and increased charge delocalization due to crystal packing. The visible-light-inducible autofluorescence serves as a complementary method to bright-field microscopy in beamline applications where accurate crystal centering about the rotation axis is essential. Owing to temperature-dependent chromophore stabilization, protein crystals exhibit tenfold higher fluorescence intensity at cryogenic temperatures, making the method ideal for experi...","publisher":"International Union of Crystallography (IUCr)","publication_date":{"day":null,"month":null,"year":2016,"errors":{}},"publication_name":"Journal of Applied Crystallography"},"translated_abstract":"Fluorescence microscopy methods have seen an increase in popularity in recent years for detecting protein crystals in screening trays. The fluorescence-based crystal detection methods have thus far relied on intrinsic UV-inducible tryptophan fluorescence, nonlinear optics or fluorescence in the visible light range dependent on crystals soaked with fluorescent dyes. In this paper data are presented on a novel visible-light-inducible autofluorescence arising from protein crystals as a result of general stabilization of conjugated double-bond systems and increased charge delocalization due to crystal packing. The visible-light-inducible autofluorescence serves as a complementary method to bright-field microscopy in beamline applications where accurate crystal centering about the rotation axis is essential. Owing to temperature-dependent chromophore stabilization, protein crystals exhibit tenfold higher fluorescence intensity at cryogenic temperatures, making the method ideal for experi...","internal_url":"https://www.academia.edu/58804540/A_visible_light_excited_fluorescence_method_for_imaging_protein_crystals_without_added_dyes","translated_internal_url":"","created_at":"2021-10-18T05:55:24.141-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":33002650,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"A_visible_light_excited_fluorescence_method_for_imaging_protein_crystals_without_added_dyes","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":33002650,"first_name":"Doletha","middle_initials":null,"last_name":"Szebenyi","page_name":"DolethaSzebenyi","domain_name":"cornell","created_at":"2015-07-12T07:19:02.115-07:00","display_name":"Doletha Szebenyi","url":"https://cornell.academia.edu/DolethaSzebenyi"},"attachments":[],"research_interests":[{"id":48,"name":"Engineering","url":"https://www.academia.edu/Documents/in/Engineering"},{"id":80414,"name":"Mathematical Sciences","url":"https://www.academia.edu/Documents/in/Mathematical_Sciences"},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences"},{"id":734874,"name":"Applied Crystallography","url":"https://www.academia.edu/Documents/in/Applied_Crystallography"}],"urls":[]}, 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="58804538"><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/58804538/Reduction_of_lattice_disorder_in_protein_crystals_by_high_pressure_cryocooling"><img alt="Research paper thumbnail of Reduction of lattice disorder in protein crystals by high-pressure cryocooling" 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" href="https://www.academia.edu/58804538/Reduction_of_lattice_disorder_in_protein_crystals_by_high_pressure_cryocooling">Reduction of lattice disorder in protein crystals by high-pressure cryocooling</a></div><div class="wp-workCard_item"><span>Journal of Applied Crystallography</span><span>, 2016</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">High-pressure cryocooling (HPC) has been developed as a technique for reducing the damage that fr...</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">High-pressure cryocooling (HPC) has been developed as a technique for reducing the damage that frequently occurs when macromolecular crystals are cryocooled at ambient pressure. Crystals are typically pressurized at around 200 MPa and then cooled to liquid nitrogen temperature under pressure; this process reduces the need for penetrating cryoprotectants, as well as the damage due to cryocooling, but does not improve the diffraction quality of the as-grown crystals. Here it is reported that HPC using a pressure above 300 MPa can reduce lattice disorder, in the form of high mosaicity and/or nonmerohedral twinning, in crystals of three different proteins, namely human glutaminase C, the GTP pyrophosphokinase YjbM and the uncharacterized protein lpg1496. Pressure lower than 250 MPa does not induce this transformation, even with a prolonged pressurization time. These results indicate that HPC at elevated pressures can be a useful tool for improving crystal packing and hence the quality o...</span></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="58804538"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="58804538"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 58804538; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=58804538]").text(description); $(".js-view-count[data-work-id=58804538]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 58804538; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='58804538']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 58804538, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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" } } $('.js-work-strip[data-work-id=58804538]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":58804538,"title":"Reduction of lattice disorder in protein crystals by high-pressure cryocooling","translated_title":"","metadata":{"abstract":"High-pressure cryocooling (HPC) has been developed as a technique for reducing the damage that frequently occurs when macromolecular crystals are cryocooled at ambient pressure. Crystals are typically pressurized at around 200 MPa and then cooled to liquid nitrogen temperature under pressure; this process reduces the need for penetrating cryoprotectants, as well as the damage due to cryocooling, but does not improve the diffraction quality of the as-grown crystals. Here it is reported that HPC using a pressure above 300 MPa can reduce lattice disorder, in the form of high mosaicity and/or nonmerohedral twinning, in crystals of three different proteins, namely human glutaminase C, the GTP pyrophosphokinase YjbM and the uncharacterized protein lpg1496. Pressure lower than 250 MPa does not induce this transformation, even with a prolonged pressurization time. These results indicate that HPC at elevated pressures can be a useful tool for improving crystal packing and hence the quality o...","publisher":"International Union of Crystallography (IUCr)","publication_date":{"day":null,"month":null,"year":2016,"errors":{}},"publication_name":"Journal of Applied Crystallography"},"translated_abstract":"High-pressure cryocooling (HPC) has been developed as a technique for reducing the damage that frequently occurs when macromolecular crystals are cryocooled at ambient pressure. Crystals are typically pressurized at around 200 MPa and then cooled to liquid nitrogen temperature under pressure; this process reduces the need for penetrating cryoprotectants, as well as the damage due to cryocooling, but does not improve the diffraction quality of the as-grown crystals. Here it is reported that HPC using a pressure above 300 MPa can reduce lattice disorder, in the form of high mosaicity and/or nonmerohedral twinning, in crystals of three different proteins, namely human glutaminase C, the GTP pyrophosphokinase YjbM and the uncharacterized protein lpg1496. Pressure lower than 250 MPa does not induce this transformation, even with a prolonged pressurization time. These results indicate that HPC at elevated pressures can be a useful tool for improving crystal packing and hence the quality o...","internal_url":"https://www.academia.edu/58804538/Reduction_of_lattice_disorder_in_protein_crystals_by_high_pressure_cryocooling","translated_internal_url":"","created_at":"2021-10-18T05:55:24.033-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":33002650,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Reduction_of_lattice_disorder_in_protein_crystals_by_high_pressure_cryocooling","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":33002650,"first_name":"Doletha","middle_initials":null,"last_name":"Szebenyi","page_name":"DolethaSzebenyi","domain_name":"cornell","created_at":"2015-07-12T07:19:02.115-07:00","display_name":"Doletha Szebenyi","url":"https://cornell.academia.edu/DolethaSzebenyi"},"attachments":[],"research_interests":[{"id":48,"name":"Engineering","url":"https://www.academia.edu/Documents/in/Engineering"},{"id":80414,"name":"Mathematical Sciences","url":"https://www.academia.edu/Documents/in/Mathematical_Sciences"},{"id":118582,"name":"Physical sciences","url":"https://www.academia.edu/Documents/in/Physical_sciences"},{"id":734874,"name":"Applied Crystallography","url":"https://www.academia.edu/Documents/in/Applied_Crystallography"}],"urls":[]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="58804536"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/58804536/Quantitative_analysis_of_Laue_diffraction_patterns_recorded_with_a_120_ps_exposure_from_an_X_ray_undulator"><img alt="Research paper thumbnail of Quantitative analysis of Laue diffraction patterns recorded with a 120 ps exposure from an X-ray undulator" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/58804536/Quantitative_analysis_of_Laue_diffraction_patterns_recorded_with_a_120_ps_exposure_from_an_X_ray_undulator">Quantitative analysis of Laue diffraction patterns recorded with a 120 ps exposure from an X-ray undulator</a></div><div class="wp-workCard_item"><span>Journal of Applied Crystallography</span><span>, 1992</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="58804536"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="58804536"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 58804536; 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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="58804532"><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/58804532/Lack_of_Catalytic_Activity_of_a_Murine_mRNA_Cytoplasmic_Serine_Hydroxymethyltransferase_Splice_Variant_Evidence_against_Alternative_Splicing_as_a_Regulatory_Mechanism_"><img alt="Research paper thumbnail of Lack of Catalytic Activity of a Murine mRNA Cytoplasmic Serine Hydroxymethyltransferase Splice Variant: Evidence against Alternative Splicing as a Regulatory Mechanism †" 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" href="https://www.academia.edu/58804532/Lack_of_Catalytic_Activity_of_a_Murine_mRNA_Cytoplasmic_Serine_Hydroxymethyltransferase_Splice_Variant_Evidence_against_Alternative_Splicing_as_a_Regulatory_Mechanism_">Lack of Catalytic Activity of a Murine mRNA Cytoplasmic Serine Hydroxymethyltransferase Splice Variant: Evidence against Alternative Splicing as a Regulatory Mechanism †</a></div><div class="wp-workCard_item"><span>Biochemistry Usa</span><span>, May 1, 2001</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Mammalian serine hydroxymethyltransferase (SHMT) is a tetrameric, pyridoxal phosphate-dependent e...</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">Mammalian serine hydroxymethyltransferase (SHMT) is a tetrameric, pyridoxal phosphate-dependent enzyme that catalyzes the reversible interconversion of serine and tetrahydrofolate to glycine and methylenetetrahydrofolate. This reaction generates single-carbon units for purine, thymidine, and methionine biosynthesis. Cytoplasmic SHMT (cSHMT) has been postulated to channel one-carbon substituted folates to various folate-dependent enzymes, and alternative splicing of the cSHMT transcript may be a mechanism that enables specific protein-protein interactions. The cytoplasmic isozyme is expressed from species-specific and tissue-specific alternatively spliced transcripts that encode proteins with modified carboxy-terminal domains, while the mitochondrial isozyme is expressed from a single transcript. While the full-length mouse and human cSHMT proteins are 91% identical, their alternatively spliced transcripts differ. The murine cSHMT gene is expressed as two transcripts. One transcript encodes a full-length 55 kDa active enzyme (cSHMT), while the other transcript encodes a 35 kDa protein (McSHMTtr). The McSHMTtr protein present in mouse liver and kidney does not bind 5-formyltetrahydrofolate, nor does it oligomerize with the full-length cSHMT enzyme. While recombinant cSHMT-glutathione S-transferase fusion proteins form tetramers and are catalytically active, McSHMTtr-glutathione S-transferase fusion proteins are catalytically inactive, do not form heterotetramers, and do not bind pyridoxal phosphate. Analysis of the murine cSHMT crystal structure indicates that the active site lysine that normally binds pyridoxal phosphate in the cSHMT protein is exposed to solvent in the McSHMTtr protein, preventing stable formation of a Schiff base with pyridoxal phosphate. Modeling studies suggest that the human cSHMT proteins expressed from alternatively spliced transcripts are inactive as well. Therefore, channeling mechanisms enabling specific protein-protein interactions of active enzymes are not based on cSHMT alternative splicing.</span></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="58804532"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="58804532"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 58804532; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=58804532]").text(description); $(".js-view-count[data-work-id=58804532]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 58804532; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='58804532']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 58804532, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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" } } $('.js-work-strip[data-work-id=58804532]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":58804532,"title":"Lack of Catalytic Activity of a Murine mRNA Cytoplasmic Serine Hydroxymethyltransferase Splice Variant: Evidence against Alternative Splicing as a Regulatory Mechanism †","translated_title":"","metadata":{"abstract":"Mammalian serine hydroxymethyltransferase (SHMT) is a tetrameric, pyridoxal phosphate-dependent enzyme that catalyzes the reversible interconversion of serine and tetrahydrofolate to glycine and methylenetetrahydrofolate. This reaction generates single-carbon units for purine, thymidine, and methionine biosynthesis. Cytoplasmic SHMT (cSHMT) has been postulated to channel one-carbon substituted folates to various folate-dependent enzymes, and alternative splicing of the cSHMT transcript may be a mechanism that enables specific protein-protein interactions. The cytoplasmic isozyme is expressed from species-specific and tissue-specific alternatively spliced transcripts that encode proteins with modified carboxy-terminal domains, while the mitochondrial isozyme is expressed from a single transcript. While the full-length mouse and human cSHMT proteins are 91% identical, their alternatively spliced transcripts differ. The murine cSHMT gene is expressed as two transcripts. One transcript encodes a full-length 55 kDa active enzyme (cSHMT), while the other transcript encodes a 35 kDa protein (McSHMTtr). The McSHMTtr protein present in mouse liver and kidney does not bind 5-formyltetrahydrofolate, nor does it oligomerize with the full-length cSHMT enzyme. While recombinant cSHMT-glutathione S-transferase fusion proteins form tetramers and are catalytically active, McSHMTtr-glutathione S-transferase fusion proteins are catalytically inactive, do not form heterotetramers, and do not bind pyridoxal phosphate. Analysis of the murine cSHMT crystal structure indicates that the active site lysine that normally binds pyridoxal phosphate in the cSHMT protein is exposed to solvent in the McSHMTtr protein, preventing stable formation of a Schiff base with pyridoxal phosphate. Modeling studies suggest that the human cSHMT proteins expressed from alternatively spliced transcripts are inactive as well. Therefore, channeling mechanisms enabling specific protein-protein interactions of active enzymes are not based on cSHMT alternative splicing.","publication_date":{"day":1,"month":5,"year":2001,"errors":{}},"publication_name":"Biochemistry Usa"},"translated_abstract":"Mammalian serine hydroxymethyltransferase (SHMT) is a tetrameric, pyridoxal phosphate-dependent enzyme that catalyzes the reversible interconversion of serine and tetrahydrofolate to glycine and methylenetetrahydrofolate. This reaction generates single-carbon units for purine, thymidine, and methionine biosynthesis. Cytoplasmic SHMT (cSHMT) has been postulated to channel one-carbon substituted folates to various folate-dependent enzymes, and alternative splicing of the cSHMT transcript may be a mechanism that enables specific protein-protein interactions. The cytoplasmic isozyme is expressed from species-specific and tissue-specific alternatively spliced transcripts that encode proteins with modified carboxy-terminal domains, while the mitochondrial isozyme is expressed from a single transcript. While the full-length mouse and human cSHMT proteins are 91% identical, their alternatively spliced transcripts differ. The murine cSHMT gene is expressed as two transcripts. One transcript encodes a full-length 55 kDa active enzyme (cSHMT), while the other transcript encodes a 35 kDa protein (McSHMTtr). The McSHMTtr protein present in mouse liver and kidney does not bind 5-formyltetrahydrofolate, nor does it oligomerize with the full-length cSHMT enzyme. While recombinant cSHMT-glutathione S-transferase fusion proteins form tetramers and are catalytically active, McSHMTtr-glutathione S-transferase fusion proteins are catalytically inactive, do not form heterotetramers, and do not bind pyridoxal phosphate. 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In part, this is because SAXS benefits greatly from the sensitivity and throughput that can be achieved at modern high brightness synchrotron sources. However, the critical need for highly monodisperse samples in SAXS analysis can be a challenge, and as such a number of labs have moved to develop in-line Size Exclusion Chromatography (SEC) at the beamline. Real-time SAXS on elution profiles not only improves monodispersity of samples and provides information on possible oligomeric states, but it also offers new modes of data analysis that can take advantage of the inherent concentration profiles underlying elution peaks and distributions of partially resolved species. Efforts to extend the synergy between SEC and SAXS to other biophysical methods are ongoing. The newly commissi...</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="b75fb6374dafd7e11c83cfbbc3c3f64a" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":73038769,"asset_id":58804527,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/73038769/download_file?st=MTczMjcyMTY1OSw4LjIyMi4yMDguMTQ2&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="58804527"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="58804527"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 58804527; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=58804527]").text(description); $(".js-view-count[data-work-id=58804527]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 58804527; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='58804527']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 58804527, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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: "b75fb6374dafd7e11c83cfbbc3c3f64a" } } $('.js-work-strip[data-work-id=58804527]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":58804527,"title":"In-line SEC-SAXS and MALS/DLS/RI for the Analysis of Polydisperse Macromolecules","translated_title":"","metadata":{"abstract":"Small Angle X-ray Scattering (SAXS) is a powerful tool for the structural analysis of biological macromolecules in solution and has seen a surge in popularity amongst structural biologists in the past decade. 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We have determined to 2.0 Å resolution the structure of Aplysia cyclase with ribose-5-phosphate bound covalently at C3′ and with the base exchange substrate (BES), pyridylcarbinol, bound to the active site. In addition, further refinement at 2.4 Å</span></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="58804526"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="58804526"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 58804526; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=58804526]").text(description); $(".js-view-count[data-work-id=58804526]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 58804526; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='58804526']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 58804526, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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" } } $('.js-work-strip[data-work-id=58804526]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":58804526,"title":"ADP-Ribosyl Cyclase","translated_title":"","metadata":{"abstract":"ADP-ribosyl cyclase catalyzes the elimination of nicotinamide from NAD and cyclization to cADPR, a known second messenger in cellular calcium signaling pathways. We have determined to 2.0 Å resolution the structure of Aplysia cyclase with ribose-5-phosphate bound covalently at C3′ and with the base exchange substrate (BES), pyridylcarbinol, bound to the active site. In addition, further refinement at 2.4 Å","publication_date":{"day":null,"month":null,"year":2004,"errors":{}},"publication_name":"Structure"},"translated_abstract":"ADP-ribosyl cyclase catalyzes the elimination of nicotinamide from NAD and cyclization to cADPR, a known second messenger in cellular calcium signaling pathways. We have determined to 2.0 Å resolution the structure of Aplysia cyclase with ribose-5-phosphate bound covalently at C3′ and with the base exchange substrate (BES), pyridylcarbinol, bound to the active site. In addition, further refinement at 2.4 Å","internal_url":"https://www.academia.edu/58804526/ADP_Ribosyl_Cyclase","translated_internal_url":"","created_at":"2021-10-18T05:55:23.218-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":33002650,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"ADP_Ribosyl_Cyclase","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":33002650,"first_name":"Doletha","middle_initials":null,"last_name":"Szebenyi","page_name":"DolethaSzebenyi","domain_name":"cornell","created_at":"2015-07-12T07:19:02.115-07:00","display_name":"Doletha Szebenyi","url":"https://cornell.academia.edu/DolethaSzebenyi"},"attachments":[],"research_interests":[{"id":3614,"name":"Structure","url":"https://www.academia.edu/Documents/in/Structure"},{"id":47884,"name":"Biological Sciences","url":"https://www.academia.edu/Documents/in/Biological_Sciences"},{"id":140081,"name":"Calcium Signaling","url":"https://www.academia.edu/Documents/in/Calcium_Signaling"},{"id":260118,"name":"CHEMICAL SCIENCES","url":"https://www.academia.edu/Documents/in/CHEMICAL_SCIENCES"},{"id":354019,"name":"Active site","url":"https://www.academia.edu/Documents/in/Active_site"},{"id":1200088,"name":"Second Messengers","url":"https://www.academia.edu/Documents/in/Second_Messengers"}],"urls":[{"id":13315672,"url":"http://sciencedirect.com/science/article/pii/s0969212604000486"}]}, 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="58804525"><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/58804525/Carbon_Dioxide_Trapped_in_a_%CE%B2_Carbonic_Anhydrase"><img alt="Research paper thumbnail of Carbon Dioxide “Trapped” in a β-Carbonic Anhydrase" 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" href="https://www.academia.edu/58804525/Carbon_Dioxide_Trapped_in_a_%CE%B2_Carbonic_Anhydrase">Carbon Dioxide “Trapped” in a β-Carbonic Anhydrase</a></div><div class="wp-workCard_item"><span>Biochemistry</span><span>, 2015</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Carbonic anhydrases (CAs) are enzymes that catalyze the hydration/dehydration of CO2/HCO3(-) with...</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">Carbonic anhydrases (CAs) are enzymes that catalyze the hydration/dehydration of CO2/HCO3(-) with rates approaching diffusion-controlled limits (kcat/KM ∼ 10(8) M(-1) s(-1)). This family of enzymes has evolved disparate protein folds that all perform the same reaction at near catalytic perfection. Presented here is a structural study of a β-CA (psCA3) expressed in Pseudomonas aeruginosa, in complex with CO2, using pressurized cryo-cooled crystallography. The structure has been refined to 1.6 Å resolution with Rcryst and Rfree values of 17.3 and 19.9%, respectively, and is compared with the α-CA, human CA isoform II (hCA II), the only other CA to have CO2 captured in its active site. Despite the lack of structural similarity between psCA3 and hCA II, the CO2 binding orientation relative to the zinc-bound solvent is identical. In addition, a second CO2 binding site was located at the dimer interface of psCA3. Interestingly, all β-CAs function as dimers or higher-order oligomeric states, and the CO2 bound at the interface may contribute to the allosteric nature of this family of enzymes or may be a convenient alternative binding site as this pocket has been previously shown to be a promiscuous site for a variety of ligands, including bicarbonate, sulfate, and phosphate ions.</span></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="58804525"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="58804525"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 58804525; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=58804525]").text(description); $(".js-view-count[data-work-id=58804525]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 58804525; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='58804525']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 58804525, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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" } } $('.js-work-strip[data-work-id=58804525]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":58804525,"title":"Carbon Dioxide “Trapped” in a β-Carbonic Anhydrase","translated_title":"","metadata":{"abstract":"Carbonic anhydrases (CAs) are enzymes that catalyze the hydration/dehydration of CO2/HCO3(-) with rates approaching diffusion-controlled limits (kcat/KM ∼ 10(8) M(-1) s(-1)). 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Interestingly, all β-CAs function as dimers or higher-order oligomeric states, and the CO2 bound at the interface may contribute to the allosteric nature of this family of enzymes or may be a convenient alternative binding site as this pocket has been previously shown to be a promiscuous site for a variety of ligands, including bicarbonate, sulfate, and phosphate ions.","publisher":"American Chemical Society (ACS)","publication_date":{"day":null,"month":null,"year":2015,"errors":{}},"publication_name":"Biochemistry"},"translated_abstract":"Carbonic anhydrases (CAs) are enzymes that catalyze the hydration/dehydration of CO2/HCO3(-) with rates approaching diffusion-controlled limits (kcat/KM ∼ 10(8) M(-1) s(-1)). This family of enzymes has evolved disparate protein folds that all perform the same reaction at near catalytic perfection. Presented here is a structural study of a β-CA (psCA3) expressed in Pseudomonas aeruginosa, in complex with CO2, using pressurized cryo-cooled crystallography. The structure has been refined to 1.6 Å resolution with Rcryst and Rfree values of 17.3 and 19.9%, respectively, and is compared with the α-CA, human CA isoform II (hCA II), the only other CA to have CO2 captured in its active site. Despite the lack of structural similarity between psCA3 and hCA II, the CO2 binding orientation relative to the zinc-bound solvent is identical. In addition, a second CO2 binding site was located at the dimer interface of psCA3. Interestingly, all β-CAs function as dimers or higher-order oligomeric states, and the CO2 bound at the interface may contribute to the allosteric nature of this family of enzymes or may be a convenient alternative binding site as this pocket has been previously shown to be a promiscuous site for a variety of ligands, including bicarbonate, sulfate, and phosphate ions.","internal_url":"https://www.academia.edu/58804525/Carbon_Dioxide_Trapped_in_a_%CE%B2_Carbonic_Anhydrase","translated_internal_url":"","created_at":"2021-10-18T05:55:23.091-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":33002650,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Carbon_Dioxide_Trapped_in_a_β_Carbonic_Anhydrase","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":33002650,"first_name":"Doletha","middle_initials":null,"last_name":"Szebenyi","page_name":"DolethaSzebenyi","domain_name":"cornell","created_at":"2015-07-12T07:19:02.115-07:00","display_name":"Doletha Szebenyi","url":"https://cornell.academia.edu/DolethaSzebenyi"},"attachments":[],"research_interests":[{"id":145,"name":"Biochemistry","url":"https://www.academia.edu/Documents/in/Biochemistry"},{"id":4594,"name":"Carbon Dioxide","url":"https://www.academia.edu/Documents/in/Carbon_Dioxide"},{"id":33441,"name":"Macromolecular X-Ray Crystallography","url":"https://www.academia.edu/Documents/in/Macromolecular_X-Ray_Crystallography"},{"id":225499,"name":"Pseudomonas aeruginosa","url":"https://www.academia.edu/Documents/in/Pseudomonas_aeruginosa"},{"id":636395,"name":"Pseudomonas Aeruginosa","url":"https://www.academia.edu/Documents/in/Pseudomonas_Aeruginosa-1"},{"id":653665,"name":"Protein Conformation","url":"https://www.academia.edu/Documents/in/Protein_Conformation"},{"id":784076,"name":"Species Specificity","url":"https://www.academia.edu/Documents/in/Species_Specificity"},{"id":956752,"name":"Protein Quaternary Structure","url":"https://www.academia.edu/Documents/in/Protein_Quaternary_Structure"},{"id":990417,"name":"Recombinant Proteins","url":"https://www.academia.edu/Documents/in/Recombinant_Proteins"},{"id":1222191,"name":"Ligands","url":"https://www.academia.edu/Documents/in/Ligands"},{"id":1681026,"name":"Biochemistry and cell biology","url":"https://www.academia.edu/Documents/in/Biochemistry_and_cell_biology"},{"id":3789880,"name":"Medical biochemistry and metabolomics","url":"https://www.academia.edu/Documents/in/Medical_biochemistry_and_metabolomics"}],"urls":[]}, dispatcherData: dispatcherData }); 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