Publication: Crystallization and preliminary X-ray crystallographic analysis of a full-length active form of the Cry4Ba toxin from Bacillus thuringiensis
Issued Date
2010-06-10
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ISSN
17443091
17443091
17443091
Other identifier(s)
2-s2.0-77953165304
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Mahidol University
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SCOPUS
Bibliographic Citation
Acta Crystallographica Section F: Structural Biology and Crystallization Communications. Vol.66, No.6 (2010), 721-724
Suggested Citation
Niramon Thamwiriyasati, Somsri Sakdee, Phimonphan Chuankhayan, Gerd Katzenmeier, Chun Jung Chen, Chanan Angsuthanasombat 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. Vol.66, No.6 (2010), 721-724. doi:10.1107/S1744309110015344 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/28688
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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
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.