TY - JOUR
T1 - Crystallization and preliminary X-ray diffraction analysis of membrane-bound respiratory [NiFe] hydrogenase from Hydrogenovibrio marinus
AU - Shomura, Yasuhito
AU - Hagiya, Keisuke
AU - Yoon, Ki Seok
AU - Nishihara, Hirofumi
AU - Higuchi, Yoshiki
N1 - Copyright:
Copyright 2012 Elsevier B.V., All rights reserved.
PY - 2011/7
Y1 - 2011/7
N2 - 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.
AB - 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.
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U2 - 10.1107/S1744309111019804
DO - 10.1107/S1744309111019804
M3 - Article
C2 - 21795805
AN - SCOPUS:79960941573
SN - 1744-3091
VL - 67
SP - 827
EP - 829
JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications
JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications
IS - 7
ER -