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Crystallization and preliminary X‐ray analysis of the Clostridium botulinum type D nontoxic nonhaemagglutinin
Author(s) -
Miyata Keita,
Inui Ken,
Miyashita ShinIchiro,
Sagane Yoshimasa,
Hasegawa Kimiko,
Matsumoto Takashi,
Yamano Akihito,
Niwa Koichi,
Watanabe Toshihiro,
Ohyama Tohru
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911105603x
Subject(s) - clostridium botulinum , crystallization , escherichia coli , neurotoxin , toxin , crystallography , trigonal crystal system , chemistry , microbiology and biotechnology , clostridium , stereochemistry , crystal structure , biology , biochemistry , bacteria , organic chemistry , gene , genetics
Clostridium botulinum produces botulinum neurotoxin (BoNT) as a large toxin complex assembled with nontoxic nonhaemagglutinin (NTNHA) and/or haemagglutinin components. Complex formation with NTNHA is considered to be critical in eliciting food poisoning because the complex shields the BoNT from the harsh conditions in the digestive tract. In the present study, NTNHA was expressed in Escherichia coli and crystallized. Diffraction data were collected to 3.9 Å resolution. The crystal belonged to the trigonal space group P 321 or P 3 1 21/ P 3 2 21, with unit‐cell parameters a = b = 147.85, c = 229.74 Å. The structure of NTNHA will provide insight into the assembly mechanism that produces the unique BoNT–NTNHA complex.

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