Niramon ThamwiriyasatiSomsri SakdeePhimonphan ChuankhayanGerd KatzenmeierChun Jung ChenChanan AngsuthanasombatMahidol UniversityNational Synchrotron Radiation Research Center TaiwanNational Tsing Hua UniversityNational Cheng Kung University2018-09-242018-09-242010-06-10Acta Crystallographica Section F: Structural Biology and Crystallization Communications. Vol.66, No.6 (2010), 721-72417443091174430912-s2.0-77953165304https://repository.li.mahidol.ac.th/handle/20.500.14594/28688To 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.Mahidol UniversityBiochemistry, Genetics and Molecular BiologyPhysics and AstronomyArticleSCOPUS10.1107/S1744309110015344