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

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)

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 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.

Original languageEnglish
Pages (from-to)452-455
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume66
Issue number4
DOIs
Publication statusPublished - 2010

Keywords

  • Cyanide ligands
  • Hydrogenases
  • HypF1
  • Maturation
  • NiFe cofactor

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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