title: Crystallization and preliminary X-ray crystallographic study of [NiFe]-hydrogenase maturation factor HypE from Thermococcus kodakaraensis KOD1.
abstract: The hydrogenase maturation protein HypE is involved in the biosynthesis of the CN ligands of the active-site iron of [NiFe] hydrogenases using carbamoylphosphate as a substrate. Here, the crystallization and preliminary crystallographic analysis of HypE from Thermococcus kodakaraensis KOD1 are reported. Crystals of HypE (338 amino acids, 35.9 kDa) have been obtained by the sitting-drop vapour-diffusion method using 2-methyl-2,4-pentanediol (MPD) as a precipitant. The crystals belong to space group P2(1)2(1)2, with unit-cell parameters a = 88.3, b = 45.8, c = 75.1 A. There is one HypE molecule in the asymmetric unit. A complete native X-ray diffraction data set was collected to a maximum resolution of 1.55 A at 100 K.
authors.affiliation: Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
authors.forename: Takayuki
authors.initials: T
authors.lastname: Arai
authors.forename: Satoshi
authors.initials: S
authors.lastname: Watanabe
authors.forename: Rie
authors.initials: R
authors.lastname: Matsumi
authors.forename: Haruyuki
authors.initials: H
authors.lastname: Atomi
authors.forename: Tadayuki
authors.initials: T
authors.lastname: Imanaka
authors.forename: Kunio
authors.initials: K
authors.lastname: Miki
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D006864:Hydrogenase / Q000737:chemistry* / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D015183:Restriction Mapping; D019712:Thermococcus / Q000201:enzymology*
chemical_list: D001426:Bacterial Proteins; D011994:Recombinant Proteins; C085871:hypE protein, Bacteria; C043296:nickel-iron hydrogenase; D006864:Hydrogenase