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|Title:||Crystallization and preliminary X-ray crystallographic analysis of a full-length active form of the Cry4Ba toxin from Bacillus thuringiensis|
Chun Jung Chen
National Synchrotron Radiation Research Center Taiwan
National Tsing Hua University
National Cheng Kung University
|Keywords:||Biochemistry, Genetics and Molecular Biology;Physics and Astronomy|
|Citation:||Acta Crystallographica Section F: Structural Biology and Crystallization Communications. Vol.66, No.6 (2010), 721-724|
|Abstract:||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. © International Union of Crystallography 2010.|
|Appears in Collections:||Scopus 2006-2010|
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