Open AccessCrystallization and preliminary X‐ray crystallographic analysis of the [NiFe]‐hydrogenase maturation factor HypF1 from Ralstonia eutropha H16
Author(s) -
Winter Gordon,
Dökel Simon,
Jones Anne K.,
Scheerer Patrick,
Krauss Norbert,
Höhne Wolfgang,
Friedrich Bärbel
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110006196
Subject(s) - ralstonia , crystallization , crystallography , materials science , cupriavidus necator , hydrogenase , x ray , chemistry , hydrogen , bacteria , physics , biochemistry , biology , organic chemistry , enzyme , optics , genetics , polyhydroxyalkanoates
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 I 222, with unit‐cell parameters a = 79.7, b = 91.6, c = 107.2 Å. 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 Å.