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

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INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309111019804

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资金

  1. Academia Sinica
  2. National Synchrotron Radiation Research Center (Taiwan)
  3. MEXT [20051022, 22770111, 18GS0207, 22370061, 22657031]
  4. JSPS [20580094]
  5. University of Hyogo
  6. Hyogo Science and Technology Association
  7. GCOE
  8. Japanese Aerospace Exploration Agency
  9. JST, Japan
  10. Grants-in-Aid for Scientific Research [22770111, 22121519, 22657031, 20580094, 22370061, 18GS0207] Funding Source: KAKEN

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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 angstrom, beta = 91.3 degrees, indicating that two heterodimers were present in the asymmetric unit.

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