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

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 P 2 1 2 1 2, with unit‐cell parameters a = 88.3, b = 45.8, c = 75.1 Å. 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 Å at 100 K.