Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:3309347rdf:typepubmed:Citationlld:pubmed
pubmed-article:3309347lifeskim:mentionsumls-concept:C0995408lld:lifeskim
pubmed-article:3309347lifeskim:mentionsumls-concept:C0020284lld:lifeskim
pubmed-article:3309347lifeskim:mentionsumls-concept:C0444626lld:lifeskim
pubmed-article:3309347lifeskim:mentionsumls-concept:C0441655lld:lifeskim
pubmed-article:3309347lifeskim:mentionsumls-concept:C0043309lld:lifeskim
pubmed-article:3309347lifeskim:mentionsumls-concept:C0010423lld:lifeskim
pubmed-article:3309347lifeskim:mentionsumls-concept:C2603343lld:lifeskim
pubmed-article:3309347lifeskim:mentionsumls-concept:C0439611lld:lifeskim
pubmed-article:3309347pubmed:issue4lld:pubmed
pubmed-article:3309347pubmed:dateCreated1987-11-13lld:pubmed
pubmed-article:3309347pubmed:abstractTextHydrogenase (EC 1.12) from Desulfovibrio gigas is a dimeric enzyme (26 and 62 (X 10(3) Mr) that catalyzes the reversible oxidation of molecular hydrogen. Single crystals of hydrogenase have been produced using the hanging drop method, with either PEG (polyethylene glycol) 6000 or ammonium sulfate as precipitants at pH 6.5. X-ray examination of the crystals indicates that those obtained with ammonium sulfate are suitable for structure determination to at least 3.0 A resolution when synchrotron radiation Sources are used (1 A = 0.1 nm). The crystals are monoclinic, with space group C2, and cell dimensions a = 257.0 A, b = 184.7 A, c = 148.3 A and beta = 101.3 degrees, and contain between four and ten molecules per asymmetric unit. The enzyme can be reactivated within the crystals under reducing conditions without crystal damage.lld:pubmed
pubmed-article:3309347pubmed:languageenglld:pubmed
pubmed-article:3309347pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:3309347pubmed:citationSubsetIMlld:pubmed
pubmed-article:3309347pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:3309347pubmed:statusMEDLINElld:pubmed
pubmed-article:3309347pubmed:monthJunlld:pubmed
pubmed-article:3309347pubmed:issn0022-2836lld:pubmed
pubmed-article:3309347pubmed:authorpubmed-author:FreyMMlld:pubmed
pubmed-article:3309347pubmed:authorpubmed-author:HatchikianCClld:pubmed
pubmed-article:3309347pubmed:authorpubmed-author:CambillauCClld:pubmed
pubmed-article:3309347pubmed:authorpubmed-author:NivièreVVlld:pubmed
pubmed-article:3309347pubmed:issnTypePrintlld:pubmed
pubmed-article:3309347pubmed:day20lld:pubmed
pubmed-article:3309347pubmed:volume195lld:pubmed
pubmed-article:3309347pubmed:ownerNLMlld:pubmed
pubmed-article:3309347pubmed:authorsCompleteYlld:pubmed
pubmed-article:3309347pubmed:pagination969-71lld:pubmed
pubmed-article:3309347pubmed:dateRevised2009-11-19lld:pubmed
pubmed-article:3309347pubmed:meshHeadingpubmed-meshheading:3309347-...lld:pubmed
pubmed-article:3309347pubmed:meshHeadingpubmed-meshheading:3309347-...lld:pubmed
pubmed-article:3309347pubmed:meshHeadingpubmed-meshheading:3309347-...lld:pubmed
pubmed-article:3309347pubmed:year1987lld:pubmed
pubmed-article:3309347pubmed:articleTitleCrystallization, preliminary X-ray study and crystal activity of the hydrogenase from Desulfovibrio gigas.lld:pubmed
pubmed-article:3309347pubmed:affiliationLaboratoire de Chimie Bacterienne, CNRS, Marseille, France.lld:pubmed
pubmed-article:3309347pubmed:publicationTypeJournal Articlelld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:3309347lld:pubmed