McPherson A, Jurnak F, Singh G J, Gill S S
Department of Biochemistry, University of California, Riverside 92521.
J Mol Biol. 1987 Jun 5;195(3):755-7. doi: 10.1016/0022-2836(87)90197-5.
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.
已可重复生长出适合高分辨率X射线衍射分析的晶体，该晶体来自苏云金芽孢杆菌的24000道尔顿蛋白质昆虫毒素。这种蛋白质通过插入磷脂膜表现出显著的杀虫活性，在中性pH条件下从聚乙二醇4000中结晶成长方形针状晶体。这些晶体属于空间群P4(1)，晶胞参数为a = b = 33 Å，c = 235 Å，这向我们表明该蛋白质结构主要是螺旋基序。
