Crystallographic refinement by incorporation of molecular dynamics: thermostable serine protease thermitase complexed with eglin c.

@article{Gros1989CrystallographicRB,
  title={Crystallographic refinement by incorporation of molecular dynamics: thermostable serine protease thermitase complexed with eglin c.},
  author={Piet Gros and Masao Fujinaga and Bauke W Dijkstra and Kor H. Kalk and Wim G. J. Hol},
  journal={Acta crystallographica. Section B, Structural science},
  year={1989},
  volume={45 ( Pt 5)},
  pages={488-99}
}
In order to investigate the principles of protein thermostability, the crystal structure of thermitase from Thermoactinomyces vulgaris, a thermostable member of the subtilisin family of serine proteases, has been determined in a complex with eglin c. Eglin c is a serine protease inhibitor from the leech Hirudo medicinalis. After data collection with a television area-detector diffractometer and initial structure solution by molecular-replacement methods, crystallographic refinement proceeded… CONTINUE READING