title: Purification, crystallization and preliminary crystallographic analysis of the [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough.
abstract: The [NiFeSe] hydrogenases belong to a subgroup of the [NiFe] proteins in which a selenocysteine is a ligand of the Ni. These enzymes demonstrate interesting catalytic properties, showing a very high H(2)-producing activity that is sustained in the presence of low O(2) concentrations. The purification, crystallization and preliminary X-ray diffraction analysis of the [NiFeSe] hydrogenase isolated from Desulfovibrio vulgaris Hildenborough are reported. Crystals of the soluble form of this hydrogenase were obtained using 20% PEG 1500 as a precipitant and belonged to the monoclinic space group P2(1), with unit-cell parameters a = 60.57, b = 91.05, c = 66.85 A, beta = 101.46 degrees. Using an in-house X-ray diffraction system, they were observed to diffract X-rays to 2.4 A resolution.
authors.affiliation: ITQB-Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Apartado 127, Oeiras, Portugal.
authors.forename: Marta
authors.initials: M
authors.lastname: Marques
authors.forename: Ricardo
authors.initials: R
authors.lastname: Coelho
authors.forename: Inês A C
authors.initials: IA
authors.lastname: Pereira
authors.forename: Pedro M
authors.initials: PM
authors.lastname: Matias
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D016969:Desulfovibrio vulgaris / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D006864:Hydrogenase / Q000737:chemistry* / Q000302:isolation & purification*
chemical_list: C058560:nickel-iron-selenium hydrogenase; D006864:Hydrogenase