X-ray analyses of aspartic proteinases. The three-dimensional structure at 2.1 A resolution of endothiapepsin.

@article{Blundell1990XrayAO,
  title={X-ray analyses of aspartic proteinases. The three-dimensional structure at 2.1 A resolution of endothiapepsin.},
  author={Tom L. Blundell and John A Jenkins and B. T. Sewell and Laurence H. Pearl and Jon B. Cooper and Ian J. Tickle and B Veerapandian and Steve P. Wood},
  journal={Journal of molecular biology},
  year={1990},
  volume={211 4},
  pages={919-41}
}
The molecular structure of endothiapepsin (EC 3.4.23.6), the aspartic proteinase from Endothia parasitica, has been refined to a crystallographic R-factor of 0.178 at 2.1 A resolution. The positions of 2389 protein non-hydrogen atoms have been determined and the present model contains 333 solvent molecules. The structure is bilobal, consisting of two predominantly beta-sheet domains that are related by an approximate 2-fold axis. Of approximately 170 residues, 65 are topologically equivalent… CONTINUE READING