Linked Life Data

18678940

Source:http://linkedlifedata.com/resource/pubmed/id/18678940

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pubmed-article:18678940pubmed:abstractTextThe membrane-bound [NiFe] hydrogenase is a unique metalloprotein that is able to catalyze the reversible oxidation of hydrogen to protons and electrons during a complex reaction cycle. The [NiFe] hydrogenase was isolated from the photosynthetic purple sulfur bacterium Allochromatium vinosum and its crystallization and preliminary X-ray analysis are reported. It was crystallized by the hanging-drop vapour-diffusion method using sodium citrate and imidazole as crystallization agents. The crystals belong to space group P2(1)2(1)2, with unit-cell parameters a = 205.00, b = 217.42, c = 120.44 A. X-ray diffraction data have been collected to 2.5 A resolution.lld:pubmed
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pubmed-article:18678940pubmed:monthAuglld:pubmed
pubmed-article:18678940pubmed:issn1744-3091lld:pubmed
pubmed-article:18678940pubmed:authorpubmed-author:LubitzWolfgan...lld:pubmed
pubmed-article:18678940pubmed:authorpubmed-author:OgataHideakiHlld:pubmed
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pubmed-article:18678940pubmed:pagination719-22lld:pubmed
pubmed-article:18678940pubmed:dateRevised2010-9-21lld:pubmed
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pubmed-article:18678940pubmed:articleTitlePurification, crystallization and preliminary X-ray analysis of the membrane-bound [NiFe] hydrogenase from Allochromatium vinosum.lld:pubmed
pubmed-article:18678940pubmed:affiliationMax-Planck-Institut für Bioanorganische Chemie, Stiftstrasse 34-36, D-45470 Mülheim an der Ruhr, Germany.lld:pubmed
pubmed-article:18678940pubmed:publicationTypeJournal Articlelld:pubmed