Manganese superoxide dismutase from Thermus thermophilus. A structural model refined at 1.8 A resolution.

@article{Ludwig1991ManganeseSD,
  title={Manganese superoxide dismutase from Thermus thermophilus. A structural model refined at 1.8 A resolution.},
  author={Martha L. Ludwig and Allan L. Metzger and Katherine A. Pattridge and William C. Stallings},
  journal={Journal of molecular biology},
  year={1991},
  volume={219 2},
  pages={335-58}
}
The structure of Mn(III) superoxide dismutase (Mn(III)SOD) from Thermus thermophilus, a tetramer of chains 203 residues in length, has been refined by restrained least-squares methods. The R-factor [formula: see text] for the 54,056 unique reflections measured between 10.0 and 1.8 A (96% of all possible reflections) is 0.176 for a model comprising the protein dimer and 180 bound solvents, the asymmetric unit of the P4(1)2(1)2 cell. The monomer chain forms two domains as determined by distance… CONTINUE READING

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