Crystallization and preliminary X-ray diffraction analysis of membrane-bound respiratory [NiFe] hydrogenase from Hydrogenovibrio marinus

Yasuhito Shomura, Keisuke Hagiya, Ki Suk Yoon, Hirofumi Nishihara, Yoshiki Higuchi

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Membrane-bound respiratory [NiFe] hydrogenase is an H 2-uptake enzyme found in the periplasmic space of bacteria that plays a crucial role in energy-conservation processes. The heterodimeric unit of the enzyme from Hydrogeno-vibrio marinus was purified to homogeneity using chromatographic procedures. Crystals were grown using the sitting-drop vapour-diffusion method at room temperature. Preliminary crystallographic analysis revealed that the crystals belonged to space group P2 1, with unit-cell parameters a = 75.72, b = 116.59, c = 113.40 Å, β = 91.3°, indicating that two heterodimers were present in the asymmetric unit.

Original languageEnglish
Pages (from-to)827-829
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume67
Issue number7
DOIs
Publication statusPublished - Jul 1 2011

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Crystallization
X-Ray Diffraction
X ray diffraction analysis
Moritella
enzymes
crystallization
membranes
Membranes
Periplasm
Crystals
energy conservation
Enzymes
diffraction
bacteria
crystals
homogeneity
Bacteria
Energy conservation
x rays
Vapors

All Science Journal Classification (ASJC) codes

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

Cite this

Crystallization and preliminary X-ray diffraction analysis of membrane-bound respiratory [NiFe] hydrogenase from Hydrogenovibrio marinus. / Shomura, Yasuhito; Hagiya, Keisuke; Yoon, Ki Suk; Nishihara, Hirofumi; Higuchi, Yoshiki.

In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 67, No. 7, 01.07.2011, p. 827-829.

Research output: Contribution to journalArticle

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