title: Crystallization and preliminary X-ray crystallographic analysis of the [NiFe]-hydrogenase maturation factor HypF1 from Ralstonia eutropha H16.
abstract: The hydrogenase maturation factor HypF1 is a truncated but functional version of the HypF protein. HypF is known to be involved in the supply of the CN(-) ligands of the active site of [NiFe]-hydrogenases, utilizing carbamoyl phosphate as a substrate. The first crystallization and preliminary X-ray studies of HypF1 from Ralstonia eutropha H16 are reported here. Crystals of HypF1 (394 amino acids, 40.7 kDa) were obtained by the sitting-drop vapour-diffusion technique using sodium formate as a precipitant. The crystals belonged to space group I222, with unit-cell parameters a = 79.7, b = 91.6, c = 107.2 A. Complete X-ray diffraction data sets were collected at 100 K from native crystals and from a platinum derivative to a maximum resolution of 1.65 A.
authors.affiliation: Institut für Biologie/Mikrobiologie, Humboldt-Universität zu Berlin, Chausseestrasse 117, D-10115 Berlin, Germany.
authors.forename: Gordon
authors.initials: G
authors.lastname: Winter
authors.forename: Simon
authors.initials: S
authors.lastname: Dökel
authors.forename: Anne K
authors.initials: AK
authors.lastname: Jones
authors.forename: Patrick
authors.initials: P
authors.lastname: Scheerer
authors.forename: Norbert
authors.initials: N
authors.lastname: Krauss
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Höhne
authors.forename: Bärbel
authors.initials: B
authors.lastname: Friedrich
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D020118:Cupriavidus necator / Q000201:enzymology*; D006864:Hydrogenase / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; C108878:HypF protein, Bacteria; C043296:nickel-iron hydrogenase; D006864:Hydrogenase
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