title: 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, β=91.3°, indicating that two heterodimers were present in the asymmetric unit.
authors.affiliation: Department of Life Science, Graduate School of Life Science, University of Hyogo, 3-2-1 Koto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan.
authors.forename: Yasuhito
authors.initials: Y
authors.lastname: Shomura
authors.forename: Keisuke
authors.initials: K
authors.lastname: Hagiya
authors.forename: Ki-Seok
authors.initials: KS
authors.lastname: Yoon
authors.forename: Hirofumi
authors.initials: H
authors.lastname: Nishihara
authors.forename: Yoshiki
authors.initials: Y
authors.lastname: Higuchi
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D006864:Hydrogenase / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry*; D044147:Piscirickettsiaceae / Q000201:enzymology*
chemical_list: D008565:Membrane Proteins; C043296:nickel-iron hydrogenase; D006864:Hydrogenase