Preliminary crystallographic studies of a protease-resistant botulinum neurotoxin associated protein Hn-33

Botulinum neurotoxin (BoNT) is one of the most potent toxins known. BoNT is also a food poison, which means that the toxin must survive the protease action and acidity of the gut. A group of neurotoxin‐associated proteins which are only beginning to be identified and characterized are believed to be...

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Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 1999-06, Vol.55 (6), p.1237-1239
Main Authors: Hadfield, Andrea T., Petsko, Greg, Lindo, Paul, Singh, Bal-Ram
Format: Article
Language:English
Subjects:
Bacterial Proteins
Botulinum clostridium
Botulinum Toxins - chemistry
Botulinum Toxins - metabolism
Crystallography, X-Ray
Endopeptidases - metabolism
haemagglutinin
Hemagglutinins - chemistry
Hemagglutinins - metabolism
Protein Conformation
toxins
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Summary:Botulinum neurotoxin (BoNT) is one of the most potent toxins known. BoNT is also a food poison, which means that the toxin must survive the protease action and acidity of the gut. A group of neurotoxin‐associated proteins which are only beginning to be identified and characterized are believed to be responsible for this protection. Hn‐33 is a 33 kDa polypeptide which is a major component of the type A botulinum neurotoxin complex. Crystals of Hn‐33 have been grown by vapour‐diffusion techniques. They belong to a primitive orthorhombic space group and diffract to a resolution of 2.6 Å, with unit‐cell parameters a = 130.3, b = 122.2, c = 37.2 Å.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444999004771