{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,1,13]],"date-time":"2025-01-13T10:40:19Z","timestamp":1736764819733,"version":"3.32.0"},"reference-count":35,"publisher":"International Union of Crystallography (IUCr)","issue":"5","license":[{"start":{"date-parts":[[2014,4,25]],"date-time":"2014-04-25T00:00:00Z","timestamp":1398384000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/journals.iucr.org\/services\/copyrightpolicy.html"},{"start":{"date-parts":[[2014,4,25]],"date-time":"2014-04-25T00:00:00Z","timestamp":1398384000000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/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"],"published-print":{"date-parts":[[2014,5,1]]},"abstract":"<jats:p>The protective mechanisms of<jats:italic>Deinococcus radiodurans<\/jats:italic>against primary reactive oxygen species involve nonenzymatic scavengers and a powerful enzymatic antioxidant system including catalases, peroxidases and superoxide dismutases that prevents oxidative damage. Catalase is an enzyme that is responsible for the conversion of H<jats:sub>2<\/jats:sub>O<jats:sub>2<\/jats:sub>to O<jats:sub>2<\/jats:sub>and H<jats:sub>2<\/jats:sub>O, protecting the organism from the oxidative effect of H<jats:sub>2<\/jats:sub>O<jats:sub>2<\/jats:sub>. This study reports the purification and crystallization of the DR1998 catalase from<jats:italic>D. radiodurans<\/jats:italic>. The crystals diffracted to 2.6\u2005\u00c5 resolution and belonged to space group<jats:italic>C<\/jats:italic>222<jats:sub>1<\/jats:sub>, with unit-cell parameters<jats:italic>a<\/jats:italic>= 97.33,<jats:italic>b<\/jats:italic>= 311.88,<jats:italic>c<\/jats:italic>= 145.63\u2005\u00c5, suggesting that they contain four molecules per asymmetric unit. The initial phases were determined by molecular replacement and the obtained solution shows the typical catalase quaternary structure. A preliminary model of the protein structure has been built and refinement is currently in progress.<\/jats:p>","DOI":"10.1107\/s2053230x1400764x","type":"journal-article","created":{"date-parts":[[2014,4,24]],"date-time":"2014-04-24T15:11:05Z","timestamp":1398352265000},"page":"659-662","update-policy":"https:\/\/doi.org\/10.1107\/cm_01","source":"Crossref","is-referenced-by-count":1,"title":["Purification, crystallization and phase determination of the DR1998 haem<i>b<\/i>catalase from<i>Deinococcus radiodurans<\/i>"],"prefix":"10.1107","volume":"70","author":[{"given":"Patr\u00edcia T.","family":"Borges","sequence":"first","affiliation":[]},{"given":"Cec\u00edlia S.","family":"Miranda","sequence":"additional","affiliation":[]},{"given":"Sandra P.","family":"Santos","sequence":"additional","affiliation":[]},{"given":"Jo\u00e3o N.","family":"Carita","sequence":"additional","affiliation":[]},{"given":"Carlos","family":"Fraz\u00e3o","sequence":"additional","affiliation":[]},{"given":"C\u00e9lia V.","family":"Rom\u00e3o","sequence":"additional","affiliation":[]}],"member":"329","published-online":{"date-parts":[[2014,4,25]]},"reference":[{"key":"fw5449_bb1","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1107\/S0907444909052925","volume":"66","author":"Adams","year":"2010","journal-title":"Acta Cryst. 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