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Alpha-toxin of Clostridium perfringens, cloned in Escherichia coli, has been purified and crystallized from ammonium sulphate using the hanging drop vapour diffusion method at 20 degrees C. The crystals diffract to a minimum Bragg spacing of 2.7 A, belong to the space group R32 (with a = b = 153.3 A, c = 95.4 A, alpha = beta = 90 degrees and gamma = 120 degrees) and contain a single polypeptide chain in the crystallographic unit.

Original publication

DOI

10.1006/jmbi.1994.1758

Type

Journal article

Journal

J Mol Biol

Publication Date

16/12/1994

Volume

244

Pages

648 - 650

Keywords

Bacterial Toxins, Calcium-Binding Proteins, Clostridium perfringens, Crystallization, Crystallography, X-Ray, Molecular Structure, Type C Phospholipases