Molecular dynamics refinement of a thermitase-eglin-c complex at 1.98 Å resolution and comparison of two crystal forms that differ in calcium content
- 1 November 1989
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 210 (2) , 347-367
- https://doi.org/10.1016/0022-2836(89)90336-7
Abstract
No abstract availableThis publication has 49 references indexed in Scilit:
- Crystal structure of thermitase from Thermoactinomyces vulgaris at 2.2 Å resolutionFEBS Letters, 1989
- Crystallization of thermitase, a thermostable subtilisin, from a sodium formate solution by means of an automated procedureJournal of Molecular Biology, 1989
- Crystallographic refinement by simulated annealingJournal of Molecular Biology, 1988
- Crystal structure of a complex between thermitase from Thermoactinomyces vulgaris and the leech inhibitor eglinFEBS Letters, 1988
- An efficient general-purpose least-squares refinement program for macromolecular structuresActa Crystallographica Section A Foundations of Crystallography, 1987
- Crystal and molecular structure of the inhibitor eglin from leeches in complex with subtilisin CarlsbergFEBS Letters, 1985
- Complete primary structure of thermitase from Thermoactinomyces vulgaris and its structural features related to the subtilisin‐type proteinasesFEBS Letters, 1985
- Molecular dynamics with coupling to an external bathThe Journal of Chemical Physics, 1984
- Dictionary of protein secondary structure: Pattern recognition of hydrogen‐bonded and geometrical featuresBiopolymers, 1983
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977