The 0.78 A structure of a serine protease: Bacillus lentus subtilisin.

@article{Kuhn1998The0A,
  title={The 0.78 A structure of a serine protease: Bacillus lentus subtilisin.},
  author={Peter A Kuhn and Mark Knapp and S Michael Soltis and Grant Ganshaw and Magdalena Th{\"o}ne and Richard R Bott},
  journal={Biochemistry},
  year={1998},
  volume={37 39},
  pages={13446-52}
}
Ultrahigh-resolution X-ray diffraction data from cryo-cooled, B. lentus subtilisin crystals has been collected to a resolution of 0.78 A. The refined model coordinates have a rms deviation of 0.22 A relative to the same structure determined at room temperature and 2.0 A resolution. Several regions of main-chain and side-chain disorder have been identified for 21 out of 269 residues in one polypeptide chain. Hydrogen atoms appear as significant peaks in the Fo - Fc difference electron density… CONTINUE READING

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