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COMPLEX BETWEEN THE SUBTILISIN FROM A MESOPHILIC BACTERIUM AND THE LEECH INHIBITOR EGLIN-C

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JournalACTA CRYSTALLOGRAPHICA SECTION B-STRUCTURAL SCIENCE
DatePublished - 1 Oct 1991
Volume47
Number of pages0
Pages (from-to)707
Original languageEnglish

Abstract

The alkaline proteinase from the mesophilic bacterium Bacillus mesentericus has been crystallized in a 1:1 complex with the inhibitor eglin-C from the medical leech. The crystals have cell dimensions of a = 43.0, b = 71.9, c = 48.3 angstrom and beta = 110.0-degrees and are in the space group P2(1). Three-dimensional data to 2.0 angstrom have been recorded on film from a single crystal. The orientation and position of the complex in the unit cell have been established using the refined coordinates of subtilisin Carlsberg and of eglin-C as independent models. The structure of the complex has been refined by restrained least-squares minimization. The crystallographic R factor (= SIGMA\\F(o)\-\F(c)\\/SIGMA\F(o)\) is 15.1% including two Ca2+ ions and 312 water molecules. The structure is discussed in terms of its physicochemical properties in solution and its relation to other Bacillus subtilisins.

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