Open AccessPurification, crystallization and preliminary X‐ray analysis of the membrane‐bound [NiFe] hydrogenase from Allochromatium vinosum
Author(s) -
Kellers Petra,
Ogata Hideaki,
Lubitz Wolfgang
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108019945
Subject(s) - hydrogenase , crystallization , crystallography , sulfur , chemistry , metalloprotein , electron transport chain , hydrogen , enzyme , biochemistry , organic chemistry
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 P 2 1 2 1 2, with unit‐cell parameters a = 205.00, b = 217.42, c = 120.44 Å. X‐ray diffraction data have been collected to 2.5 Å resolution.