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Crystallization and preliminary X-ray diffraction analysis of membrane-bound respiratory [NiFe] hydrogenase from Hydrogenovibrio marinus.

ABSTRACT: Membrane-bound respiratory [NiFe] hydrogenase is an H2-uptake enzyme found in the periplasmic space of bacteria that plays a crucial role in energy-conservation processes. The heterodimeric unit of the enzyme from Hydrogenovibrio marinus was purified to homogeneity using chromatographic procedures. Crystals were grown using the sitting-drop vapour-diffusion method at room temperature. Preliminary crystallographic analysis revealed that the crystals belonged to space group P2(1), with unit-cell parameters a=75.72, b=116.59, c=113.40?Å, ?=91.3°, indicating that two heterodimers were present in the asymmetric unit.

SUBMITTER: Shomura Y

PROVIDER: S-EPMC3144807 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction analysis of membrane-bound respiratory [NiFe] hydrogenase from Hydrogenovibrio marinus.

Shomura Yasuhito Y Hagiya Keisuke K Yoon Ki-Seok KS Nishihara Hirofumi H Higuchi Yoshiki Y

Acta crystallographica. Section F, Structural biology and crystallization communications 20110630 Pt 7

Membrane-bound respiratory [NiFe] hydrogenase is an H2-uptake enzyme found in the periplasmic space of bacteria that plays a crucial role in energy-conservation processes. The heterodimeric unit of the enzyme from Hydrogenovibrio marinus was purified to homogeneity using chromatographic procedures. Crystals were grown using the sitting-drop vapour-diffusion method at room temperature. Preliminary crystallographic analysis revealed that the crystals belonged to space group P2(1), with unit-cell p ...[more]

PMID: 21795805

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