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

Abstract

The crystal structure of an alkaline protease from Bacillus alcalophilus has been determined by X-ray diffraction at 2.4 ,~ resolution. The enzyme crystallizes in space group P212~21 with lattice constants a= 53.7, b= 61.6, c=75.9 .&. 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.