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Updated: Aug 12, 2026

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Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD
Published on: December 30, 2016
Purification, crystallization and preliminary X-ray diffraction studies of alpha-toxin of Clostridium perfringens
A K Basak1, D I Stuart, T Nikura
1Laboratory of Molecular Biophysics, Oxford University, U.K.
Journal of Molecular Biology
|December 16, 1994
Abstract:
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.

