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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/31371
Title: Crystallization and preliminary X-ray crystallographic analysis of the functional form of BinB binary toxin from Bacillus sphaericus
Authors: Kanokporn Srisucharitpanit
Min Yao
Sarin Chimnaronk
Boonhiang Promdonkoy
Isao Tanaka
Panadda Boonserm
Mahidol University
Hokkaido University
Thailand National Center for Genetic Engineering and Biotechnology
Keywords: Biochemistry, Genetics and Molecular Biology;Physics and Astronomy
Issue Date: 1-Feb-2013
Citation: Acta Crystallographica Section F: Structural Biology and Crystallization Communications. Vol.69, No.2 (2013), 170-173
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.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84873582525&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/31371
ISSN: 17443091
Appears in Collections:Scopus 2011-2015

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