{"id":16705,"date":"2019-07-18T11:24:05","date_gmt":"2019-07-18T09:24:05","guid":{"rendered":"https:\/\/news.embl.de\/?p=16705"},"modified":"2024-03-22T10:56:20","modified_gmt":"2024-03-22T09:56:20","slug":"first-results-from-cssb","status":"publish","type":"post","link":"https:\/\/www.embl.org\/news\/science\/first-results-from-cssb\/","title":{"rendered":"First results from CSSB"},"content":{"rendered":"\n<p>Six research groups, among them two from EMBL Hamburg, have developed a protocol that will simplify the process of solubilising integral membrane proteins (IMPs), as they report on 17 July in <em>Scientific Reports<\/em>. This is also the first publication resulting from a collaboration at the <a href=\"http:\/\/www.cssb-hamburg.de\/about_us\/index_eng.html\">Centre for Structural Systems Biology<\/a>(CSSB) in Hamburg.<\/p>\n\n\n\n<p>\u201cWorking with membrane proteins is challenging,\u201d says corresponding author and EMBL group leader Mar\u00eda Garc\u00eda Alai. \u201cWhile they\u2019re in the membrane, they\u2019re not soluble. So you have to get them out, which is the most difficult part. When you do that, you might be altering the structure of the proteins, so you never know exactly what is happening.\u201d<\/p>\n\n\n\n<p>The first step of working with IMPs is to extract them from the membrane using detergents. This can alter the protein, which then has to be purified and reintegrated into a membrane-like environment. Experimenting with different detergents to get the best result is expensive, because the detergent has to be removed in various technical steps. Garc\u00eda\u2019s team and their collaborators showed that it\u2019s possible to measure the stability and solubility of IMPs by diluting them into different detergents. The result was a protocol that allows the identification of suitable conditions for membrane proteins during purification. \u201cThis will be very useful for all the laboratories working with membrane proteins. We show a lot of evidence that this pipeline is the way to go,\u201d says Garc\u00eda.<\/p>\n\n\n\n<p>The development of the protocol is the first result of a collaboration between various research groups using the Protein Characterisation facility at CSSB. Inaugurated in 2017, CSSB is a cooperation involving nine research partners from Northern Germany, including three universities and six research institutes. CSSB aims to become a leading international research centre studying the structure and function of pathogens. The first two facilities running at the site are the High-Throughput Crystallisation facility and the Protein Characterisation facility, both provided by EMBL.<\/p>\n\n\n\n<p>\u201cOne of the most important things about the CSSB concept is that we\u2019re not only doing research, but also contributing with facilities for the scientific community,\u201d says Garc\u00eda Alai. \u201cAll the different scientific institutions that are part of CSSB work together and push forward the infrastructure, facilities and scientific services. And this is the first result.\u201d<\/p>\n\n\n\n<p>The groups working on the project include the <a href=\"https:\/\/www.embl-hamburg.de\/research\/unit\/garcia-alai\/index.html\">Garc\u00eda Alai team<\/a> and the <a href=\"https:\/\/www.embl-hamburg.de\/research\/unit\/loew\/index.html\">L\u00f6w group<\/a>, both at EMBL Hamburg, and their collaborators. The paper will be included in a special collection issued by S<em>cientific Reports&nbsp;<\/em>called \u2018Structure and mechanism of membrane transporters\u2019.<\/p>\n","protected":false},"excerpt":{"rendered":"<p>EMBL scientists collaborate to develop new protocol for screening membrane protein stability<\/p>\n","protected":false},"author":69,"featured_media":16707,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"footnotes":""},"categories":[2,17591],"tags":[474,775,11421,53,461,704,51],"embl_taxonomy":[],"class_list":["post-16705","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-science","category-science-technology","tag-collaboration","tag-cssb","tag-garcia-alai","tag-hamburg","tag-low","tag-proteins","tag-systems-biology"],"acf":{"article_intro":"<p>EMBL scientists collaborate to develop new protocol for screening membrane protein stability<\/p>\n","related_links":[{"link_description":"CSSB Website","link_url":"http:\/\/www.cssb-hamburg.de"}],"article_sources":[{"source_description":"<p>Garc\u00eda Alai\u00a0<em>et al.\u00a0<\/em>High-throughput stability screening for detergent-solubilized membrane proteins, <em>Scientific Reports<\/em>. Published online\u00a017 July 2019. DOI:\u00a0https:\/\/doi.org\/10.1038\/s41598-019-46686-8<\/p>\n","source_link_url":"https:\/\/doi.org\/10.1038\/s41598-019-46686-8"}],"vf_locked":false,"featured":false,"color":"#007B53","show_featured_image":false,"field_target_display":"","in_this_article":false,"press_contact":"None","translations":false},"embl_taxonomy_terms":[],"yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v26.2 - https:\/\/yoast.com\/wordpress\/plugins\/seo\/ -->\n<title>First results from CSSB | EMBL<\/title>\n<meta name=\"description\" content=\"Scientists collaborate to develop new protocol for screening membrane protein stability at the Centre for Structural Systems Biology (CSSB)\" \/>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/www.embl.org\/news\/science\/first-results-from-cssb\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" 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