Article
Crystallization and preliminary X-ray crystallographic analysis of a full-length active form of the Cry4Ba toxin from Bacillus thuringiensis.
Acta crystallographica. Section F, Structural biology and crystallization communications - 1 Jun 2010
Thamwiriyasati Niramon, Sakdee Somsri, Chuankhayan Phimonphan, Katzenmeier Gerd, Chen Chun Jung, Angsuthanasombat Chanan
Abstract excerpt
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,...
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