Purification, crystallization and preliminary X-ray diffraction studies of alpha-toxin of Clostridium perfringens.
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.
Basak
A K
AK
Laboratory of Molecular Biophysics, Oxford University, U.K.
Stuart
D I
DI
Nikura
T
T
Bishop
D H
DH
Kelly
D C
DC
Fearn
A
A
Titball
R W
RW
D001427:Bacterial Toxins / Q000737:chemistry* / Q000302:isolation & purification; D002135:Calcium-Binding Proteins; D003016:Clostridium perfringens / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D015394:Molecular Structure; D010738:Type C Phospholipases
D001427:Bacterial Toxins; D002135:Calcium-Binding Proteins; D010738:Type C Phospholipases; C040649:alpha toxin, Clostridium perfringens