{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,30]],"date-time":"2026-07-30T11:12:46Z","timestamp":1785409966653,"version":"3.56.0"},"reference-count":26,"publisher":"International Union of Crystallography (IUCr)","issue":"2","license":[{"start":{"date-parts":[[2026,1,13]],"date-time":"2026-01-13T00:00:00Z","timestamp":1768262400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/journals.iucr.org\/services\/copyrightpolicy.html"},{"start":{"date-parts":[[2026,1,13]],"date-time":"2026-01-13T00:00:00Z","timestamp":1768262400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.iucr.org\/services\/copyrightpolicy.html#TDM"}],"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":[[2026,1,6]]},"published-print":{"date-parts":[[2026,2,1]]},"abstract":"<jats:p>\n                    The XPD helicase plays a critical role in DNA repair and serves as a model for structural studies of superfamily 2 (SF2) helicases. We report a novel orthorhombic crystal form of DNA-free\n                    <jats:italic>Thermoplasma acidophilum<\/jats:italic>\n                    XPD (TaXPD) obtained under high ionic strength conditions generated by sodium potassium tartrate and NaCl-based vapor-diffusion conditions, in contrast to earlier previously reported conditions that used polyols (PEG) or diols (MPD). The crystals belonged to space group\n                    <jats:italic>P<\/jats:italic>\n                    2\n                    <jats:sub>1<\/jats:sub>\n                    2\n                    <jats:sub>1<\/jats:sub>\n                    2\n                    <jats:sub>1<\/jats:sub>\n                    (\n                    <jats:italic>a<\/jats:italic>\n                    = 59.53,\n                    <jats:italic>b<\/jats:italic>\n                    = 96.00,\n                    <jats:italic>c<\/jats:italic>\n                    = 159.09\u2005\u00c5) and diffracted to 2.13\u2005\u00c5 resolution, yielding the highest resolution TaXPD structure to date. Structural analysis showed that this crystal form contains fewer intermolecular interfaces than the previously reported hexagonal lattice, as supported by\n                    <jats:italic>Protein Interfaces, Surfaces and Assemblies<\/jats:italic>\n                    (\n                    <jats:italic>PISA<\/jats:italic>\n                    ) analysis. This supports the determination of the 510\u2013514 loop in the long-form DNA-free TaXPD, which was previously disordered in other structures. This work highlights how crystallization conditions influence lattice organization, structural completeness and diffraction quality. In this structure, Tyr425 adopts a conformation that may regulate DNA access in the DNA-free state.\n                  <\/jats:p>","DOI":"10.1107\/s2053230x26000105","type":"journal-article","created":{"date-parts":[[2026,1,9]],"date-time":"2026-01-09T11:01:38Z","timestamp":1767956498000},"page":"42-48","update-policy":"https:\/\/doi.org\/10.1107\/cm_01","source":"Crossref","is-referenced-by-count":0,"title":["A new crystal form of the DNA-free full-length XPD helicase from\n                    <i>Thermoplasma acidophilum<\/i>"],"prefix":"10.1107","volume":"82","author":[{"given":"Marco","family":"Bravo","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/03nawhv43","id-type":"ROR","asserted-by":"publisher"}],"department":["Department of Biochemistry"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Li","family":"Fan","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/03nawhv43","id-type":"ROR","asserted-by":"publisher"}],"department":["Department of Biochemistry"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"329","published-online":{"date-parts":[[2026,1,13]]},"reference":[{"key":"or5038_bb1","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/j.ymeth.2011.07.005","volume":"55","author":"Adams","year":"2011","journal-title":"Methods"},{"key":"or5038_bb2","doi-asserted-by":"crossref","first-page":"3613","DOI":"10.1074\/jbc.M113.523001","volume":"289","author":"Buechner","year":"2014","journal-title":"J. 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