Acta Crystallographica Section F 2008-08-01

Purification, crystallization and preliminary X-ray analysis of the membrane-bound [NiFe] hydrogenase from Allochromatium vinosum.

Petra Kellers, Hideaki Ogata, Wolfgang Lubitz

Index: Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64(Pt 8) , 719-22, (2008)

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Abstract

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.

Related Compounds

  • Mineral oil
  • Chymotrypsin

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