Purification, crystallization and preliminary X-ray analysis ofBacteroides fragilisZn2+β-lactamase
- 1 July 1997
- journal article
- research article
- Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section D-Biological Crystallography
- Vol. 53 (4) , 485-487
- https://doi.org/10.1107/s0907444997000966
Abstract
The Zn(2+) beta-lactamase from Bacteroides fragilis (E.C. 3.5.2.6) was overexpressed in Escherichia coli using an isopropylthiogalactoside-inducible T7 RNA polymerase expression system. Crystallization trials by the hanging-drop vapour-diffusion method have yielded two different crystal forms from two slightly different conditions. Crystals of form I belong to the monoclinic space group C2 with unit-cell dimensions a = 56.03, b = 43.98, c = 105.32 A, beta = 112 degrees and diffracted only up to 4.0 A. Crystals of form II are orthorhombic, space group P2(1)2(1)2(1) with unit-cell dimensions a = 48.10, b = 98.05, c = 111.76 A, diffract to at least 2.0 A and are suitable for high-resolution structural analysis.Keywords
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