{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,8]],"date-time":"2026-09-08T05:01:01Z","timestamp":1788843661813,"version":"build-2803163510"},"reference-count":27,"publisher":"Wiley","issue":"S1","license":[{"start":{"date-parts":[[2016,3,28]],"date-time":"2016-03-28T00:00:00Z","timestamp":1459123200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Proteins"],"published-print":{"date-parts":[[2016,9]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:p>Hybrid approaches combine computational methods with experimental data. The information contained in the experimental data can be leveraged to probe the structure of proteins otherwise elusive to computational methods. Compared with computational methods, the structures produced by hybrid methods exhibit some degree of experimental validation. In spite of these advantages, most hybrid methods have not yet been validated in blind tests, hampering their development. Here, we describe the first blind test of a specific cross\u2010link based hybrid method in CASP. This blind test was coordinated by the CASP organizers and utilized a novel, high\u2010density cross\u2010linking\/mass\u2010spectrometry (CLMS) approach that is able to collect high\u2010density CLMS data in a matter of days. This experimental protocol was developed in the Rappsilber laboratory. This approach exploits the chemistry of a highly reactive, photoactivatable cross\u2010linker to produce an order of magnitude more cross\u2010links than homobifunctional cross\u2010linkers. The Rappsilber laboratory generated experimental CLMS data based on this protocol, submitted the data to the CASP organizers which then released this data to the CASP11 prediction groups in a separate, CLMS assisted modeling experiment. We did not observe a clear improvement of assisted models, presumably because the properties of the CLMS data\u2014uncertainty in cross\u2010link identification and residue\u2010residue assignment, and uneven distribution over the protein\u2014were largely unknown to the prediction groups and their approaches were not yet tailored to this kind of data. We also suggest modifications to the CLMS\u2010CASP experiment and discuss the importance of rigorous blind testing in the development of hybrid methods. Proteins 2016; 84(Suppl 1):152\u2013163. \u00a9 2016 The Authors Proteins: Structure, Function, and Bioinformatics Published by Wiley Periodicals, Inc.<\/jats:p>","DOI":"10.1002\/prot.25028","type":"journal-article","created":{"date-parts":[[2016,3,6]],"date-time":"2016-03-06T08:45:54Z","timestamp":1457253954000},"page":"152-163","source":"Crossref","is-referenced-by-count":28,"title":["Blind testing of cross\u2010linking\/mass spectrometry hybrid methods in CASP11"],"prefix":"10.1002","volume":"84","author":[{"given":"Michael","family":"Schneider","sequence":"first","affiliation":[{"name":"Robotics and Biology Laboratory Technische Universit\u00e4t Berlin 10587 Berlin Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Adam","family":"Belsom","sequence":"additional","affiliation":[{"name":"Wellcome Trust Centre for Cell Biology University of Edinburgh Edinburgh EH9 3BF United 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