{"id":7419,"date":"2016-08-30T17:00:44","date_gmt":"2016-08-30T15:00:44","guid":{"rendered":"http:\/\/news.embl.de\/?p=7419"},"modified":"2025-05-12T11:41:34","modified_gmt":"2025-05-12T09:41:34","slug":"1608-time-resolved-crystallography","status":"publish","type":"post","link":"https:\/\/www.embl.org\/news\/science\/1608-time-resolved-crystallography\/","title":{"rendered":"Taking crystallography to the fourth dimension"},"content":{"rendered":"\n

\u201cNow we have the right people, in the right place, with the right technology!\u201d exclaims EMBL group leader Thomas Schneider, who coordinates activities at the EMBL crystallography beamlines on DESY\u2019s light source PETRA III in Hamburg. Together with Arwen Pearson, Professor at the Centre for Ultrafast Imaging (CUI), Universit\u00e4t Hamburg, he and his team have been laying the groundwork to take crystallography \u2013 his structural biology method of choice \u2013 into a new time dimension.<\/p>\n\n\n\n

Crystallography uses powerful X-ray beams to probe the 3D atomic structure of biological molecules such as proteins. As the X-rays bounce off the atoms in the protein, a distinctive pattern is produced that reveals information about its structure. This information can help scientists understand not only what a protein looks like, but also how it works and interacts with other molecules. \u201cCrystallography gives us a single snapshot of a molecule in a single state,\u201d explains Pearson. \u201cIf you\u2019re lucky, your data will also allow you to see how it is bound to another molecule and you can begin to extrapolate how that molecule works.\u201d But sometimes one structure alone is not enough.<\/p>\n\n\n\n

What we really want to do is to watch this process in motion<\/p><\/blockquote>\n\n\n\n

The whole of the protein can be involved in a binding event and any subsequent chemical reaction, and it changes shape as the molecules lock into place. \u201cBut just how the entire structure moves and changes shape is not really understood,\u201d says Pearson. \u201cWhat we really want to do is to watch this process in motion.\u201d Instead of just one snapshot, time-resolved crystallography involves taking many snapshots in quick succession to create a film of the molecule in motion, similar to running many photos together to make a movie.<\/p>\n\n\n\n

\"Viewing<\/a>
Time-resolved crystallography allows scientists to study how a protein’s shape changes during a reaction. Scientists use lasers to trigger the reaction, and then an X-ray beam to capture a series of snapshots of the protein as the reactions unfolds. They can then put those snapshots together to create a movie of the molecule in action. View and download the infographic<\/a>. IMAGE: gobius.pt<\/figcaption><\/figure><\/div>\n\n\n\n

Time-resolved crystallography is still very much a niche method, with complex requirements for both sample preparation and experimental set-up. Even defining when everything starts \u2013 Time Zero \u2013 is tricky. The reaction has to be triggered by a \u201cpump\u201d \u2013 a light pulse or a temperature jump for instance. \u201cJust imagine me giving you a push,\u201d says Pearson. \u201cThe push, or pump, triggers you to start falling over, and we can watch what happens when you do. That push defines Time Zero.\u201d As the protein starts to move, the X-ray beam is used to probe the 3D structure of the protein at regular intervals thereafter, capturing information about the structure at different stages of the process.<\/p>\n\n\n\n

This \u201cpump-probe\u201d concept won Ronald George Wreyford Norrish, George Porter and Manfred Eigen a Nobel Prize in Chemistry in 1967 and is widely used in time-resolved experiments. Some naturally light-sensitive proteins, like those involved in vision, can be easily triggered using bright laser pulses. Otherwise, a \u2018reaction initiation strategy\u2019 must be painstakingly worked out for each new protein. Once this has been established, the crystallographic experiment itself requires a very bright X-ray source and clever strategies to ensure data of sufficient quality are obtained. These issues are the current focus of Pearson\u2019s research at the CUI and will be central themes for the new Hamburg Advanced Research Centre for Bioorganic Chemistry (HARBOR), which is being coordinated by Pearson and is soon to be established at the Universit\u00e4t Hamburg.<\/p>\n\n\n\n

New dimensions<\/h2>\n\n\n\n

The beamlines at EMBL Hamburg at DESY\u2019s light source PETRA III have precisely the right qualities for taking crystallography into this next time dimension. \u201cIn order to take many snapshots in quick succession, you need a really small, stable and brilliant beam,\u201d explains Schneider. \u201cHere we really profit from the excellent properties of PETRA III, and the EMBL crystallography beamline P14 that translates the beam delivered by PETRA III into what we need for these types of experiments.\u201d<\/p>\n\n\n\n

To catch a process in action, you also need to be able to work on the same timescale at which the reaction occurs. \u201cWith the new European X-ray Free Electron Laser being built here in Hamburg, we will be able to observe extremely fast chemical reactions,\u201d explains Pearson. \u201cBut we are also interested in watching mechanistic structural changes \u2013 these occur on timescales that are already accessible to us at the beamlines. Currently, we can see reactions that occur in the millisecond range, but plans are afoot to further optimise the beamline so we can start to look at fascinating events happening on nano- and microsecond timescales.\u201d With grant funding from the German Federal Ministry for Education and Research, the groups will be able to extend the EMBL beamline P14 to establish an additional endstation dedicated to time-resolved crystallography.<\/p>\n\n\n\n

\"Arwen
Arwen Pearson and Thomas Schneider are laying groundwork to take crystallography to a new dimension. PHOTO: EMBL\/Rosemary Wilson<\/figcaption><\/figure>\n\n\n\n

Coming together<\/h2>\n\n\n\n

It was a talk by Pearson at the European Crystallography Meeting held in Warwick, UK in 2013 that got Schneider thinking and made him realise that time-resolved experiments might actually be possible on the EMBL crystallography beamlines at PETRA III. Discussions then really kicked off a year later when Pearson took up her post as Professor at the CUI, just across the road from the EMBL beamlines on the DESY campus. \u201cThe facilities at PETRA III were the reason I came to Hamburg!\u201d says Pearson with a smile. \u201cHamburg is currently the epicentre of time-resolved science, and is the place to do these types of experiments,\u201d she adds excitedly.<\/p>\n\n\n\n

We are the gadget guys!<\/p><\/blockquote>\n\n\n\n

But the ongoing development and establishment of the technique in Hamburg wouldn\u2019t be possible without the dedication of many people behind the scenes, say Schneider and Pearson \u2013 from the EMBL beamline Project Evaluation Committee who recognised the unique opportunity, to the instrumentation teams based in both Hamburg and Grenoble who provide dedicated support to the project. \u201cTime-resolved crystallography is by no means standard, and it is crucial to have the support and expertise of people like Gleb Bourenkov, a principle beamline scientist at P14 who has tested different set-ups on the beamline,\u201d says Pearson.<\/p>\n\n\n\n

Pearson and Schneider are already working with several groups who are interested in studying the dynamics of their samples \u2013 but this is just the start. \u201cWe will be able to help scientists choose the right initiation switch for their system in preparation for experiments at the EMBL beamlines and ultimately the dedicated endstation,\u201d Pearson explains. \u201cWe want to provide the best beamline facilities and services so that scientists can study the dynamics of their proteins in detail,\u201d adds Schneider, grinning. \u201cWe are the gadget guys!\u201d<\/p>\n","protected":false},"excerpt":{"rendered":"

Collaborating to take crystallography into a new time dimension<\/p>\n","protected":false},"author":18,"featured_media":7423,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"footnotes":""},"categories":[2,17591],"tags":[29,53,69,409,35,19503,13664],"embl_taxonomy":[],"class_list":["post-7419","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-science","category-science-technology","tag-crystallography","tag-hamburg","tag-methods","tag-schneider","tag-structural-biology","tag-t-rexx","tag-time-resolved-crystallography"],"acf":{"article_intro":"

Crystallography, but not as we know it<\/p>\n","related_links":[{"link_description":"","link_url":""},{"link_description":"","link_url":""}],"article_sources":false,"vf_locked":false,"featured":false,"color":"#007B53","link_color":"#fff","show_featured_image":false,"in_this_article":false,"youtube_url":"","mp4_url":"","video_caption":"","press_contact":"None","field_target_display":"embl","source_article":false,"vfwp-news_embl_taxonomy":false,"field_article_language":{"value":"english","label":"English"},"article_translations":false,"languages":""},"embl_taxonomy_terms":[],"yoast_head":"\nTaking crystallography to the fourth dimension | EMBL<\/title>\n<meta name=\"description\" content=\"Scientists at EMBL in Hamburg and Universit\u00e4t Hamburg have been laying the groundwork to take crystallography into a new time dimension.\" \/>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" 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