Crystallization and preliminary X-ray diffraction studies of the lepidopteran-specific insecticidal crystal protein CrylA(a).
A trypsin-activated CrylA(a) protein from Bacillus thuringiensis has been purified and crystallized. Crystals belong to orthorhombic space group P2(1)2(1)2(1), with cell dimensions a = 53.3, b = 111.3 and c = 154.7 A. The crystals diffract to at least 2.2 angstrum resolution and are suitable for X-ray structural analysis. They contain a single molecule in the asymmetric unit.
Biotechnology Research Institute, National Research Council of Canada, Montreal, Quebec.
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Borisova
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Grochulski
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H
van Faassen
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Pusztai-Carey
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Masson
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Cygler
D000818:Animals; D001413:Bacillus thuringiensis / Q000737:chemistry*; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D001427:Bacterial Toxins; D003460:Crystallization; D018360:Crystallography, X-Ray; D004731:Endotoxins / Q000737:chemistry* / Q000235:genetics; D006460:Hemolysin Proteins; D007915:Lepidoptera; D015394:Molecular Structure; D011994:Recombinant Proteins / Q000096:biosynthesis
D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D004731:Endotoxins; D006460:Hemolysin Proteins; D011994:Recombinant Proteins; C030956:insecticidal crystal protein, Bacillus Thuringiensis