{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,30]],"date-time":"2026-07-30T13:37:01Z","timestamp":1785418621061,"version":"3.56.0"},"reference-count":0,"publisher":"International Union of Crystallography (IUCr)","issue":"5","license":[{"start":{"date-parts":[[2026,4,23]],"date-time":"2026-04-23T00:00:00Z","timestamp":1776902400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/legalcode"},{"start":{"date-parts":[[2026,4,23]],"date-time":"2026-04-23T00:00:00Z","timestamp":1776902400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/legalcode"}],"funder":[{"DOI":"10.13039\/100014943","name":"Sarepta Therapeutics","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100014943","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R35-GM118047"],"award-info":[{"award-number":["R35-GM118047"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["iucr.org","wiley.com","iucrj.org"],"crossmark-restriction":true},"short-container-title":["Acta Crystallogr F Struct Biol Commun","Acta Crystallogr F","Acta Crystallogr F Struct Biol Cryst Commun","Acta Cryst F","Acta Cryst F Struct Biol Commun","Acta Cryst Sect F","Acta Cryst Sect F Struct Biol Commun","Acta Crystallogr Sect F","Acta Crystallogr Sect F Struct Biol Commun","Acta Crystallogr Sect F Struct Biol Cryst Commun"],"accepted":{"date-parts":[[2026,3,26]]},"published-print":{"date-parts":[[2026,5,1]]},"abstract":"<jats:p>\n                    The structure of spectrin-like repeat 24 of human dystrophin was determined at 2.5\u2005\u00c5 effective resolution. The structure exhibits a three-helix bundle fold, common to all spectrin-repeat family members, and shares a high degree of homology with existing structures of spectrin-like repeat 1 from dystrophin and utrophin. The structure provides molecular details of the atomic interactions that stabilize the repeat, including hydrophobic interactions and inter-helix and intra-helix salt bridges.\n                    <jats:italic>AlphaFold<\/jats:italic>\n                    models of the repeat are in excellent agreement with the structure, showing an all-atom r.m.s.d. of 1.13\u2005\u00c5. Accurate modeling of SR24 supports\n                    <jats:italic>AlphaFold<\/jats:italic>\n                    modeling of all 24 of the dystrophin spectrin-like repeats and the use of these models in predicting the molecular determinants of dystrophin stability, a key aspect of its biological function as a structural protein that cross-links actin filaments to the dystrophin\u2013glycoprotein complex to mediate a mechanical connection between the cytoskeleton and the extracellular matrix.\n                  <\/jats:p>","DOI":"10.1107\/s2053230x26003262","type":"journal-article","created":{"date-parts":[[2026,4,20]],"date-time":"2026-04-20T14:12:41Z","timestamp":1776694361000},"page":"184-193","update-policy":"https:\/\/doi.org\/10.1107\/cm_01","source":"Crossref","is-referenced-by-count":0,"title":["The atomic structure of human dystrophin spectrin-like repeat 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Biophysics"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"suffix":"III","given":"Robert","family":"Evans","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/017zqws13","id-type":"ROR","asserted-by":"publisher"}],"department":["Department of Biochemistry, Molecular Biology, and Biophysics"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joseph M.","family":"Muretta","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/017zqws13","id-type":"ROR","asserted-by":"publisher"}],"department":["Department of Biochemistry, Molecular Biology, and Biophysics"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"329","published-online":{"date-parts":[[2026,4,23]]},"container-title":["Acta Crystallographica Section F Structural Biology 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