Crystallization and preliminary X-ray crystallographic analysis of the [NiFe]-hydrogenase maturation factor HypF1 from Ralstonia eutropha H16.

Gordon Winter, Simon Dökel, Anne K Jones, Patrick Scheerer, Norbert Krauss, Wolfgang Höhne, Bärbel Friedrich

Acta crystallographica. Section F, Structural biology and crystallization communications 2010 Apr 01

filter terms:

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.

Citation

Gordon Winter, Simon Dökel, Anne K Jones, Patrick Scheerer, Norbert Krauss, Wolfgang Höhne, Bärbel Friedrich. Crystallization and preliminary X-ray crystallographic analysis of the [NiFe]-hydrogenase maturation factor HypF1 from Ralstonia eutropha H16. Acta crystallographica. Section F, Structural biology and crystallization communications. 2010 Apr 01;66(Pt 4):452-5