产气荚膜梭菌α毒素的纯化、结晶及初步X射线衍射研究
Purification, crystallization and preliminary X-ray diffraction studies of alpha-toxin of Clostridium perfringens.
作者信息
Basak A K, Stuart D I, Nikura T, Bishop D H, Kelly D C, Fearn A, Titball R W
机构信息
Laboratory of Molecular Biophysics, Oxford University, U.K.
出版信息
J Mol Biol. 1994 Dec 16;244(5):648-50. doi: 10.1006/jmbi.1994.1758.
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.
在大肠杆菌中克隆的产气荚膜梭菌α毒素，已通过在20℃下采用悬滴气相扩散法从硫酸铵中进行纯化和结晶。这些晶体的最小布拉格间距为2.7 Å，属于空间群R32（a = b = 153.3 Å，c = 95.4 Å，α = β = 90°，γ = 120°），并且在晶胞中含有一条单一的多肽链。
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