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

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

Research output: Contribution to journalArticle

5 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

Fingerprint

formic acid
Cupriavidus necator
Carbamyl Phosphate
Hydrogenase
Crystallization
Platinum
X-Ray Diffraction
Catalytic Domain
X-Rays
crystallization
Ligands
Amino Acids
X rays
Crystals
crystals
Proteins
x rays
formates
amino acids
phosphates

Keywords

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

ASJC Scopus subject areas

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

Cite this

Crystallization and preliminary X-ray crystallographic analysis of the [NiFe]-hydrogenase maturation factor HypF1 from Ralstonia eutropha H16. / Winter, Gordon; Dökel, Simon; Jones, Anne Katherine; Scheerer, Patrick; Krauss, Norbert; Höhne, Wolfgang; Friedrich, Bärbel.

In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 66, No. 4, 2010, p. 452-455.

Research output: Contribution to journalArticle

@article{90a8916e34ca49ad97f8c0ee880f0578,
title = "Crystallization and preliminary X-ray crystallographic analysis of the [NiFe]-hydrogenase maturation factor HypF1 from Ralstonia eutropha H16",
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 {\AA}. 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 {\AA}.",
keywords = "Cyanide ligands, Hydrogenases, HypF1, Maturation, NiFe cofactor",
author = "Gordon Winter and Simon D{\"o}kel and Jones, {Anne Katherine} and Patrick Scheerer and Norbert Krauss and Wolfgang H{\"o}hne and B{\"a}rbel Friedrich",
year = "2010",
doi = "10.1107/S1744309110006196",
language = "English",
volume = "66",
pages = "452--455",
journal = "Acta Crystallographica Section F:Structural Biology Communications",
issn = "1744-3091",
publisher = "John Wiley and Sons Ltd",
number = "4",

}

TY - JOUR

T1 - Crystallization and preliminary X-ray crystallographic analysis of the [NiFe]-hydrogenase maturation factor HypF1 from Ralstonia eutropha H16

AU - Winter, Gordon

AU - Dökel, Simon

AU - Jones, Anne Katherine

AU - Scheerer, Patrick

AU - Krauss, Norbert

AU - Höhne, Wolfgang

AU - Friedrich, Bärbel

PY - 2010

Y1 - 2010

N2 - 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.

AB - 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.

KW - Cyanide ligands

KW - Hydrogenases

KW - HypF1

KW - Maturation

KW - NiFe cofactor

UR - http://www.scopus.com/inward/record.url?scp=77950832722&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77950832722&partnerID=8YFLogxK

U2 - 10.1107/S1744309110006196

DO - 10.1107/S1744309110006196

M3 - Article

VL - 66

SP - 452

EP - 455

JO - Acta Crystallographica Section F:Structural Biology Communications

JF - Acta Crystallographica Section F:Structural Biology Communications

SN - 1744-3091

IS - 4

ER -