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Peptide binding and exchange occurs in the endoplasmic reticulum in a sequence of events mediated by the chaperones tapasin and TAPBPR (see the Perspective by Cresswell). Thomas and Tamp\u00e9 resolved the crystal structure of the TAPBPR-MHC I editing complex by using a photocleavable high-affinity peptide to stabilize the MHC molecule. Jiang\n                    <jats:italic>et al.<\/jats:italic>\n                    crystalized MHC I molecules inhabited by truncated disulfide-linked peptides that still permit TAPBPR to bind. These complimentary snapshots elucidate the dynamic process by which chaperones stabilize the groove of peptide-free MHC I molecules. This helps MHC I sample peptide candidates and facilitates the generation of peptide repertoires enriched with high-affinity antigenic peptides.\n                  <\/jats:p>\n                  <jats:p>\n                    <jats:italic>Science<\/jats:italic>\n                    , this issue p.\n                    <jats:related-article xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"doi\" issue=\"6366\" page=\"1060\" related-article-type=\"in-this-issue\" vol=\"358\" xlink:href=\"10.1126\/science.aao6001\">1060<\/jats:related-article>\n                    , p.\n                    <jats:related-article xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"doi\" issue=\"6366\" page=\"1064\" related-article-type=\"in-this-issue\" vol=\"358\" xlink:href=\"10.1126\/science.aao5154\">1064<\/jats:related-article>\n                    ; see also p.\n                    <jats:related-article xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"doi\" issue=\"6366\" page=\"992\" related-article-type=\"in-this-issue\" vol=\"358\" xlink:href=\"10.1126\/science.aaq1398\">992<\/jats:related-article>\n                  <\/jats:p>","DOI":"10.1126\/science.aao6001","type":"journal-article","created":{"date-parts":[[2017,10,12]],"date-time":"2017-10-12T21:10:37Z","timestamp":1507842637000},"page":"1060-1064","source":"Crossref","is-referenced-by-count":132,"title":["Structure of the TAPBPR\u2013MHC I complex defines the mechanism of peptide loading and editing"],"prefix":"10.1126","volume":"358","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-7441-1089","authenticated-orcid":false,"given":"Christoph","family":"Thomas","sequence":"first","affiliation":[{"name":"Institute of Biochemistry, Biocenter, Goethe University Frankfurt, Max-von-Laue Strasse 9, 60438 Frankfurt\/Main, Germany."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0403-2160","authenticated-orcid":false,"given":"Robert","family":"Tamp\u00e9","sequence":"additional","affiliation":[{"name":"Institute of Biochemistry, Biocenter, Goethe University Frankfurt, Max-von-Laue Strasse 9, 60438 Frankfurt\/Main, Germany."},{"name":"Cluster of Excellence\u2013Macromolecular Complexes, Goethe University Frankfurt, Max-von-Laue Strasse 9, 60438 Frankfurt\/Main, 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