Crystallization and preliminary X-ray crystallographic analysis of the [NiFe]-hydrogenase maturation factor HypF1 from Ralstonia eutropha H16.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 66(Pt 4): 452-5, 2010 Apr 01.
Article
em En
| MEDLINE
| ID: mdl-20383020
ABSTRACT
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.
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Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
/
Cupriavidus necator
/
Hidrogenase
Idioma:
En
Ano de publicação:
2010
Tipo de documento:
Article