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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 8
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pubmed:dateCreated |
2008-8-5
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pubmed:abstractText |
The 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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678940-10555572,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678940-12121756,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678940-15243788,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678940-15299374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678940-1540647,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678940-16271886,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678940-16893172,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678940-17304591,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678940-17845059,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678940-17845060,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678940-17847093,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678940-17850165,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678940-17927155,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678940-17927158,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678940-17927159,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678940-7803444,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678940-7854413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678940-7984417,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678940-9228943,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678940-9757107,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18678940-9920874
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1744-3091
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
64
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
719-22
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pubmed:dateRevised |
2010-9-21
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pubmed:meshHeading |
pubmed-meshheading:18678940-Chromatography, Gel,
pubmed-meshheading:18678940-Crystallization,
pubmed-meshheading:18678940-Crystallography, X-Ray,
pubmed-meshheading:18678940-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:18678940-Hydrogenase,
pubmed-meshheading:18678940-Protein Conformation,
pubmed-meshheading:18678940-Proteobacteria,
pubmed-meshheading:18678940-Spectrometry, Mass, Matrix-Assisted Laser...
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pubmed:year |
2008
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pubmed:articleTitle |
Purification, crystallization and preliminary X-ray analysis of the membrane-bound [NiFe] hydrogenase from Allochromatium vinosum.
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pubmed:affiliation |
Max-Planck-Institut für Bioanorganische Chemie, Stiftstrasse 34-36, D-45470 Mülheim an der Ruhr, Germany.
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pubmed:publicationType |
Journal Article
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