Literature DB >> 7990145

Purification, crystallization and preliminary X-ray diffraction studies of alpha-toxin of Clostridium perfringens.

A K Basak1, D I Stuart, T Nikura, D H Bishop, D C Kelly, A Fearn, R W Titball.   

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.

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Year:  1994        PMID: 7990145     DOI: 10.1006/jmbi.1994.1758

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  2 in total

1.  Use of site-directed mutagenesis to probe structure-function relationships of alpha-toxin from Clostridium perfringens.

Authors:  I Guillouard; T Garnier; S T Cole
Journal:  Infect Immun       Date:  1996-07       Impact factor: 3.441

2.  Phylogenetic analysis of phospholipase C genes from Clostridium perfringens types A to E and Clostridium novyi.

Authors:  K Tsutsui; J Minami; O Matsushita; S Katayama; Y Taniguchi; S Nakamura; M Nishioka; A Okabe
Journal:  J Bacteriol       Date:  1995-12       Impact factor: 3.490

  2 in total

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