Crystal structure of an alkaline protease from Bacillus alcalophilus at 2.4 Å resolution

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Abstract

The crystal structure of an alkaline protease from Bacillus alcahphilus has been determined by X-ray diffraction at 2.4 Å resolution. The enzyme crystallizes in space group P212121, with lattice constants a = 53.7, b = 61.6, c = 75.9 Å. 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. © 1990.

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Sobek, H., Hecht, H. J., Hofmann, B., Aehle, W., & Schomburg, D. (1990). Crystal structure of an alkaline protease from Bacillus alcalophilus at 2.4 Å resolution. FEBS Letters, 274(1–2), 57–60. https://doi.org/10.1016/0014-5793(90)81328-L

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