Crystallization and Preliminary X-ray Analysis of NADH:rubredoxin Oxidoreductase from Clostridium acetobutylicum
Crystallization and Preliminary X-ray Analysis of NADH:rubredoxin Oxidoreductase from Clostridium acetobutylicum
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丙酮丁醇梭菌 NADH:红氧还蛋白氧化还原酶的结晶和初步 X 射线分析
DOI:
10.1107/s1744309109047162
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发表时间:
2010
期刊:
影响因子:
--
通讯作者:
Y. Niimura and Y. Higuchi
中科院分区:
文献类型:
--
作者:
K. Nishikawa;Y. Shomura;S. Kawasaki;Y. Niimura and Y. Higuchi
NADH:rubredoxin oxidoreductase (NROR), an O2-inducible protein, is a versatile electron donor for scavengers of O2 and reactive oxygen species (ROS) in Clostridium acetobutylicum. Recombinant NROR was overexpressed in Escherichia coli and purified to homogeneity; it was subsequently crystallized using the sitting-drop vapour-diffusion method at 293 K. Preliminary crystallographic analysis revealed that the crystals belonged to space group P4122 or P4322, with unit-cell parameters a = b = 98.6, c = 88.3 Å, and diffracted to 2.1 Å resolution. Assuming that the crystals contained one molecule per asymmetric unit, the Matthews coefficient was calculated to be 2.7 Å3 Da−1 and the solvent content to be 54.1%.