Crystal structure of an alkaline protease from Bacillus alcalophilus at 2.4Åresolution
Open Access
- 12 November 1990
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 274 (1-2) , 57-60
- https://doi.org/10.1016/0014-5793(90)81328-l
Abstract
The crystal structure of an alkaline protease from Bacillus alcahphilus has been determined by X‐ray diffraction at 2.4Åresolution. The enzyme crystallizes in space group P212121, with lattice constants a = 53.7, b = 61.6, c = 75.9Å. The structure was solved by molecular replacement using the structure of subtilisin Carlsberg as search model. Refinement using molecular dynamics and restrained least squares methods results in a crystallographic R‐factor of 0.185. The tertiary structure is very similar to that of subtilisin Carlsberg. The greatest structural differences occur in loops at the surface of the protein.Keywords
This publication has 24 references indexed in Scilit:
- The use of an imaging proportional counter in macromolecular crystallographyJournal of Applied Crystallography, 1987
- Relation between structure and function of α/β–protejnsQuarterly Reviews of Biophysics, 1980
- A structure-factor least-squares refinement procedure for macromolecular structures using constrainedandrestrained parametersActa Crystallographica Section A, 1977
- Serine Proteases: Structure and Mechanism of CatalysisAnnual Review of Biochemistry, 1977
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977
- Subtilisin Novo. The Three-Dimensional Structure and Its Comparison with Subtilisin BPN'European Journal of Biochemistry, 1972
- Structure of Subtilisin BPN′ at 2.5 Å ResolutionNature, 1969
- A method of positioning a known molecule in an unknown crystal structureActa Crystallographica, 1967
- The detection of sub-units within the crystallographic asymmetric unitActa Crystallographica, 1962