Crystal structure of an alkaline protease from Bacillus alcalophilus at 2.4Åresolution

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 P2 12 12 1, with lattice constants a = 53.7, b = 61.6, c = 75.9Å. The structure was solved by molecular replacement using the str...

Full description

Saved in:
Bibliographic Details
Published in:FEBS letters 1990-11, Vol.274 (1), p.57-60
Main Authors: Sobek, H., Hecht, H.J., Hofmann, B., Aehle, W., Schomburg, D.
Format: Article
Language:English
Subjects:
Alkaline protease
Bacillus alcalophilus
Crystal structure
Crystallization
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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 P2 12 12 1, 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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(90)81328-L