Preliminary crystallographic studies of a protease-resistant botulinum neurotoxin associated protein Hn-33
Andrea T. Hadfield, Greg Petsko, Paul Lindo, Bal-Ram Singh
Abstract
Andrea T. Hadfield, Greg Petsko, Paul Lindo, Bal-Ram Singh
Abstract
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 A, with unit-cell parameters a = 130.3, b = 122.2, c = 37.2 A.
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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 A, with unit-cell parameters a = 130.3, b = 122.2, c = 37.2 A.
Key concepts: Neurotoxin, Botulinum neurotoxin, Orthorhombic crystal system, Protease, Clostridium botulinum, Toxin, Chemistry, Protease inhibitor (pharmacology)