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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 P6(2)22, 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.

SUBMITTER: Srisucharitpanit K 

PROVIDER: S-EPMC3564622 | biostudies-literature | 2013 Feb

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray crystallographic analysis of the functional form of BinB binary toxin from Bacillus sphaericus.

Srisucharitpanit Kanokporn K   Yao Min M   Chimnaronk Sarin S   Promdonkoy Boonhiang B   Tanaka Isao I   Boonserm Panadda P  

Acta crystallographica. Section F, Structural biology and crystallization communications 20130131 Pt 2


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 P6(2)22, with unit-cell parameters a = b = 95.2, c = 154.9 Å. Se  ...[more]

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