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Crystallization and preliminary X-ray analysis of NADH:rubredoxin oxidoreductase from Clostridium acetobutylicum

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INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309109047162

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  1. GCOE Program
  2. Japanese Aerospace Exploration Agency Project
  3. Grant-in-Aid for Scientific Research [18GS0207]
  4. JST, Japan

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NADH: rubredoxin oxidoreductase (NROR), an O-2-inducible protein, is a versatile electron donor for scavengers of O-2 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 P4(1)22 or P4(3)22, with unit-cell parameters a = b = 98.6, c = 88.3 angstrom, and diffracted to 2.1 angstrom resolution. Assuming that the crystals contained one molecule per asymmetric unit, the Matthews coefficient was calculated to be 2.7 angstrom(3) Da(-1) and the solvent content to be 54.1%.

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