The structure of horse methaemoglobin at 2-0 A resolution.

@article{Ladner1977TheSO,
  title={The structure of horse methaemoglobin at 2-0 A resolution.},
  author={R. Ladner and E. J. Heidner and M. Perutz},
  journal={Journal of molecular biology},
  year={1977},
  volume={114 3},
  pages={
          385-414
        }
}
Abstract The structure of horse methaemoglobin has been redetermined by phase extension and refinement. This has improved our knowledge of the haem geometry and the stereochemistry of the interfaces between the subunits, and confirmed the disorder of the C-terminal residues. Using new four-circle diffractometer data between the limiting spheres of radius 10 and 2.0 A −1 , the co-ordinates determined by Perutz et al. (1968 a,b ) were subjected to successive cycles of real-space refinement into… Expand
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