
Clostridium botulinumproduces 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 inEscherichia coliand crystallized. Diffraction data were collected to 3.9 Å resolution. The crystal belonged to the trigonal space groupP321 orP3121/P3221, with unit-cell parametersa=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.
Bacterial Proteins, Clostridium botulinum type D, Crystallization, Crystallography, X-Ray
Bacterial Proteins, Clostridium botulinum type D, Crystallization, Crystallography, X-Ray
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