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diffraction</a></div></div><div class="u-pb4x u-mt3x"><div class="summary u-fs14 u-fw300 u-lineHeight1_5 u-tcGrayDarkest"><div class="summarized">An emulsion-based serial crystallographic technology has been developed, in which nanolitre-sized droplets of protein solution are encapsulated in oil and stabilized by surfactant. Once the first crystal in a drop is nucleated, the small... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_58804511" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">An emulsion-based serial crystallographic technology has been developed, in which nanolitre-sized droplets of protein solution are encapsulated in oil and stabilized by surfactant. Once the first crystal in a drop is nucleated, the small volume generates a negative feedback mechanism that lowers the supersaturation. This mechanism is exploited to produce one crystal per drop. Diffraction data are measured, one crystal at a time, from a series of room-temperature crystals stored on an X-ray semi-transparent microfluidic chip, and a 93% complete data set is obtained by merging single diffraction frames taken from different unoriented crystals. As proof of concept, the structure of glucose isomerase was solved to 2.1 Å, demonstrating the feasibility of high-throughput serial X-ray crystallography using synchrotron radiation.</div></div></div><ul class="InlineList u-ph0x u-fs13"><li class="InlineList-item logged_in_only"><div class="share_on_academia_work_button"><a class="academia_share Button Button--inverseBlue Button--sm js-bookmark-button" data-academia-share="Work/58804511" data-share-source="work_strip" data-spinner="small_white_hide_contents"><i class="fa fa-plus"></i><span class="work-strip-link-text u-ml1x" data-content="button_text">Bookmark</span></a></div></li><li class="InlineList-item"><div class="download"><a id="bbc741e061a3cb629460cf93a24261b9" rel="nofollow" data-download="{&quot;attachment_id&quot;:73038771,&quot;asset_id&quot;:58804511,&quot;asset_type&quot;:&quot;Work&quot;,&quot;always_allow_download&quot;:false,&quot;track&quot;:null,&quot;button_location&quot;:&quot;work_strip&quot;,&quot;source&quot;:null,&quot;hide_modal&quot;:null}" class="Button Button--sm Button--inverseGreen js-download-button prompt_button doc_download" href="https://www.academia.edu/attachments/73038771/download_file?st=MTczMjcxNDU5Myw4LjIyMi4yMDguMTQ2&s=work_strip"><i class="fa fa-arrow-circle-o-down fa-lg"></i><span class="u-textUppercase u-ml1x" data-content="button_text">Download</span></a></div></li><li class="InlineList-item"><ul class="InlineList InlineList--bordered u-ph0x"><li class="InlineList-item InlineList-item--bordered"><span class="InlineList-item-text">by&nbsp;<span itemscope="itemscope" itemprop="author" itemtype="https://schema.org/Person"><a class="u-tcGrayDark u-fw700" data-has-card-for-user="33002650" href="https://cornell.academia.edu/DolethaSzebenyi">Doletha Szebenyi</a><script data-card-contents-for-user="33002650" type="text/json">{"id":33002650,"first_name":"Doletha","last_name":"Szebenyi","domain_name":"cornell","page_name":"DolethaSzebenyi","display_name":"Doletha Szebenyi","profile_url":"https://cornell.academia.edu/DolethaSzebenyi","photo":"/images/s65_no_pic.png"}</script></span></span></li><li class="js-paper-rank-work_58804511 InlineList-item InlineList-item--bordered hidden"><span class="js-paper-rank-view hidden u-tcGrayDark" data-paper-rank-work-id="58804511"><i class="u-m1x fa fa-bar-chart"></i><strong class="js-paper-rank"></strong></span><script>$(function() { new Works.PaperRankView({ workId: 58804511, container: ".js-paper-rank-work_58804511", }); 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solution and has seen a surge in popularity amongst structural biologists in the past decade. In part, this is because SAXS... <a class="more_link u-tcGrayDark u-linkUnstyled" data-container=".work_58804527" data-show=".complete" data-hide=".summarized" data-more-link-behavior="true" href="#">more</a></div><div class="complete hidden">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. 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. 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