Sobek H, Hecht H J, Hofmann B, Aehle W, Schomburg D
Gesellschaft für Biotechnologische Forschung, Braunschweig, FRG.
FEBS Lett. 1990 Nov 12;274(1-2):57-60. doi: 10.1016/0014-5793(90)81328-l.
The crystal structure of an alkaline protease from Bacillus alcalophilus has been determined by X-ray diffraction at 2.4 A resolution. The enzyme crystallizes in space group P2(1)2(1)2(1) with lattice constants a = 53.7, b = 61.6, c = 75.9 A. 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.
