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Crystallization and preliminary X-ray crystallographic study of [NiFe]-hydrogenase maturation factor HypE from Thermococcus kodakaraensis KOD1.

Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.2007 Sep 01;63(Pt 9):765-7. Epub 2007 Aug 25
Takayuki Arai 1 , Satoshi Watanabe , Rie Matsumi , Haruyuki Atomi , Tadayuki Imanaka , Kunio Miki
Takayuki Arai 1 , Satoshi Watanabe , Rie Matsumi , Haruyuki Atomi , Tadayuki Imanaka , Kunio Miki
+ et al

[No authors listed]

Author information
  • 1 Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.

摘要


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.