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Alternative methods have been developed that are often combined with computational methods in hybrid structural biology strategies. Among these, the combination of chemical cross-linking and MS (XL-MS) has shown to be particularly informative. Current XL-MS methods mainly rely on the coupling of lysine residues. Here we describe a chemistry to cross-link acidic residues that generates structural information complementary to that obtained by amine-specific cross-linking, thus significantly expanding the scope of XL-MS analyses.<\/jats:p>","DOI":"10.1073\/pnas.1320298111","type":"journal-article","created":{"date-parts":[[2014,6,18]],"date-time":"2014-06-18T04:24:18Z","timestamp":1403065458000},"page":"9455-9460","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":247,"title":["Chemical cross-linking\/mass spectrometry targeting acidic residues in proteins and protein complexes"],"prefix":"10.1073","volume":"111","author":[{"given":"Alexander","family":"Leitner","sequence":"first","affiliation":[{"name":"Department of Biology, Institute of Molecular Systems Biology, Eidgen\u00f6ssische Technische Hochschule Z\u00fcrich, 8093 Zurich, Switzerland;"}]},{"given":"Lukasz A.","family":"Joachimiak","sequence":"additional","affiliation":[{"name":"Department of Biology, Stanford University, Stanford, CA 94305;"}]},{"given":"Pia","family":"Unverdorben","sequence":"additional","affiliation":[{"name":"Department of Molecular Structural Biology, Max-Planck-Institute of Biochemistry, 82152 Martinsried, Germany; and"}]},{"given":"Thomas","family":"Walzthoeni","sequence":"additional","affiliation":[{"name":"Department of Biology, Institute of Molecular Systems Biology, Eidgen\u00f6ssische Technische Hochschule Z\u00fcrich, 8093 Zurich, Switzerland;"}]},{"given":"Judith","family":"Frydman","sequence":"additional","affiliation":[{"name":"Department of Biology, Stanford University, Stanford, CA 94305;"}]},{"given":"Friedrich","family":"F\u00f6rster","sequence":"additional","affiliation":[{"name":"Department of Molecular Structural Biology, Max-Planck-Institute of Biochemistry, 82152 Martinsried, Germany; and"}]},{"given":"Ruedi","family":"Aebersold","sequence":"additional","affiliation":[{"name":"Department of Biology, Institute of Molecular Systems Biology, Eidgen\u00f6ssische Technische Hochschule Z\u00fcrich, 8093 Zurich, Switzerland;"},{"name":"Faculty of Science, University of Zurich, 8057 Zurich, Switzerland"}]}],"member":"341","published-online":{"date-parts":[[2014,6,17]]},"reference":[{"key":"e_1_3_3_1_2","doi-asserted-by":"publisher","DOI":"10.1255\/ejms.1178"},{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1074\/mcp.R111.014027"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.sbi.2013.02.008"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1074\/mcp.R000001-MCP201"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jsb.2010.10.014"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1071\/CH13164"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1038\/emboj.2009.401"},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.1021\/pr200260n"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/gks220"},{"key":"e_1_3_3_10_2","doi-asserted-by":"publisher","DOI":"10.7554\/eLife.00005"},{"key":"e_1_3_3_11_2","doi-asserted-by":"publisher","DOI":"10.1038\/ncomms2985"},{"key":"e_1_3_3_12_2","doi-asserted-by":"publisher","DOI":"10.1002\/pmic.201100516"},{"key":"e_1_3_3_13_2","doi-asserted-by":"publisher","DOI":"10.1021\/pr3011638"},{"key":"e_1_3_3_14_2","doi-asserted-by":"publisher","DOI":"10.1074\/mcp.M112.024497"},{"key":"e_1_3_3_15_2","doi-asserted-by":"publisher","DOI":"10.1021\/ac101586z"},{"key":"e_1_3_3_16_2","doi-asserted-by":"publisher","DOI":"10.1074\/mcp.M112.019562"},{"key":"e_1_3_3_17_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jsb.2012.04.016"},{"key":"e_1_3_3_18_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi301069r"},{"key":"e_1_3_3_19_2","doi-asserted-by":"publisher","DOI":"10.1021\/ac302860m"},{"key":"e_1_3_3_20_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.cbpa.2012.10.034"},{"key":"e_1_3_3_21_2","first-page":"D43","article-title":"Update on activities at the Universal Protein Resource (UniProt) in 2013","volume":"41","author":"Apweiler R","year":"2013","unstructured":"R Apweiler, et al., Update on activities at the Universal Protein Resource (UniProt) in 2013. 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