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Preliminary X-ray diffraction analysis of crystals of Bacillus thuringiensis toxin, a cell membrane disrupting
A McPherson1, F Jurnak, G J Singh
1Department of Biochemistry, University of California, Riverside 92521.
Journal of Molecular Biology
|June 5, 1987
Abstract:
Crystals suitable for high resolution X-ray diffraction analysis have been reproducibly grown of the 24,000 Mr protein insect toxin from Bacillus thuringiensis. This protein, which demonstrates substantial insecticidal activity by inserting into phospholipid membranes, crystallizes as long square needles from polyethylene glycol 4000 at neutral pH. The crystals are of space group P4(1) and have cell dimensions of a = b = 33 A and c = 235 A, which suggests to us a predominantly helical motif for the protein's structure.