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Crystallization and preliminary X‐ray crystallographic analysis of a full‐length active form of the Cry4Ba toxin from Bacillus thuringiensis

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To obtain a complete structure of the Bacillus thuringiensis Cry4Ba mosquito‐larvicidal protein, a 65 kDa functional form of the Cry4Ba‐R203Q mutant toxin was generated for crystallization by eliminating the tryptic cleavage site at Arg203. The 65 kDa trypsin‐resistant fragment was purified and crystallized using the sitting‐drop vapour‐diffusion method. The crystals belonged to the rhombohedral space group R32, with unit‐cell parameters a = b = 184.62, c = 187.36 Å. Diffraction data were collected to at least 2.07 Å resolution using synchrotron radiation and gave a data set with an overall R merge of 9.1% and a completeness of 99.9%. Preliminary analysis indicated that the asymmetric unit contained one molecule of the active full‐length mutant, with a V M coefficient and solvent content of 4.33 Å3 Da−1 and 71%, respectively.
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Keywords: Bacillus thuringiensis; Cry4Ba mosquito‐larvicidal protein

Document Type: Research Article

Publication date: June 1, 2010

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