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dc.contributor.authorCabanos, Cerroneen
dc.contributor.authorUrabe, Hiroyukien
dc.contributor.authorMasuda, Taroen
dc.contributor.authorTandang-Silvas, Mary Roseen
dc.contributor.authorUtsumi, Shigeruen
dc.contributor.authorMikami, Bunzoen
dc.contributor.authorMaruyama, Nobuyukien
dc.contributor.alternative丸山, 伸之ja
dc.date.accessioned2010-11-24T00:52:22Z-
dc.date.available2010-11-24T00:52:22Z-
dc.date.issued2010-09-01-
dc.identifier.issn1744-3091-
dc.identifier.urihttp://hdl.handle.net/2433/131796-
dc.description.abstractPeanuts contain some of the most potent food allergens known to date. Ara h 1 is one of the three major peanut allergens. As a first step towards three-dimensional structure elucidation, recombinant Ara h 1 core region was cloned, expressed in Escherichia coli and purified to homogeneity. Crystals were obtained using 0.1 M sodium citrate pH 5.6, 0.1 M NaCl, 15% PEG 400 as precipitant. The crystals diffracted to 2.25 A resolution using synchrotron radiation and belonged to the monoclinic space group C2, with unit-cell parameters a=156.521, b=88.991, c=158.971 A, beta=107.144 degrees. Data were collected at the BL-38B1 station of SPring-8 (Hyogo, Japan).en
dc.format.mimetypeapplication/pdf-
dc.language.isoeng-
dc.publisherInternational Union of Crystallographyen
dc.rights© International Union of Crystallographyen
dc.subjectpeanut allergensen
dc.subjectAra h 1en
dc.titleCrystallization and preliminary X-ray analysis of the major peanut allergen Ara h 1 core region.en
dc.typejournal article-
dc.type.niitypeJournal Article-
dc.identifier.ncidAA12097708-
dc.identifier.jtitleActa crystallographica. Section F, Structural biology and crystallization communicationsen
dc.identifier.volume66-
dc.identifier.issuePt 9-
dc.identifier.spage1071-
dc.identifier.epage1073-
dc.relation.doi10.1107/S1744309110029040-
dc.textversionpublisher-
dc.identifier.pmid20823529-
dcterms.accessRightsopen access-
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