期刊
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
卷 67, 期 -, 页码 827-829出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309111019804
关键词
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资金
- Academia Sinica
- National Synchrotron Radiation Research Center (Taiwan)
- MEXT [20051022, 22770111, 18GS0207, 22370061, 22657031]
- JSPS [20580094]
- University of Hyogo
- Hyogo Science and Technology Association
- GCOE
- Japanese Aerospace Exploration Agency
- JST, Japan
- Grants-in-Aid for Scientific Research [22770111, 22121519, 22657031, 20580094, 22370061, 18GS0207] Funding Source: KAKEN
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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