Abstract
The C-terminal fragment ( M r, 21,800) of colicin A (a bacterial toxin that kills sensitive Escherichia coli cells) has been crystallized. This fragment, which possesses the pore-forming activity of the toxin, resulted from thermolysin digestion of the entire molecule. The crystals are tetragonal, space group P4 12 12 ( or P4 32 12) with a = b = 72.8 A ̊ , c = 170.4 A ̊ They contain a dimer in the asymmetric unit and diffract to 2.7 Å.
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