Publication: Crystallization and preliminary X-ray crystallographic analysis of the functional form of BinB binary toxin from Bacillus sphaericus
Issued Date
2013-02-01
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ISSN
17443091
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2-s2.0-84873582525
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Mahidol University
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SCOPUS
Bibliographic Citation
Acta Crystallographica Section F: Structural Biology and Crystallization Communications. Vol.69, No.2 (2013), 170-173
Suggested Citation
Kanokporn Srisucharitpanit, Min Yao, Sarin Chimnaronk, Boonhiang Promdonkoy, Isao Tanaka, Panadda Boonserm Crystallization and preliminary X-ray crystallographic analysis of the functional form of BinB binary toxin from Bacillus sphaericus. Acta Crystallographica Section F: Structural Biology and Crystallization Communications. Vol.69, No.2 (2013), 170-173. doi:10.1107/S1744309113000110 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/31371
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Title
Crystallization and preliminary X-ray crystallographic analysis of the functional form of BinB binary toxin from Bacillus sphaericus
Abstract
The binary toxin from Bacillus sphaericus consists of two proteins, BinA and BinB, which work together to exert toxicity against mosquito larvae. BinB is proposed to be a receptor-binding domain and internalizes BinA into the midgut cells, resulting in toxicity via an unknown mechanism. The functional form of BinB has been successfully crystallized. The crystals of BinB diffracted to a resolution of 1.75 Å and belong to space group P6222, with unit-cell parameters a = b = 95.2, c = 154.9 Å. Selenomethionine-substituted BinB (SeMetBinB) was prepared and crystallized for experimental phasing. The SeMetBinB crystal data were collected at a wavelength of 0.979 Å and diffracted to a resolution of 1.85 Å. © 2013 International Union of Crystallography All rights reserved.