» Articles » PMID: 1762156

Crystallization and Preliminary X-ray Analysis of Botulinum Neurotoxin Type A

Overview
Journal J Mol Biol
Publisher Elsevier
Date 1991 Dec 20
PMID 1762156
Citations 4
Authors
Affiliations
Soon will be listed here.
Abstract

Botulinum neurotoxin serotype A was isolated from liquid culture of Clostridium botulinum. The pure Mr approximately 150,000 neurotoxin, composed of Mr approximately 50,000 light and Mr approximately 100,000 heavy chains, has been crystallized in three different crystal morphologies; all three have the same crystal form. The most suitable crystal form for X-ray analysis are bipyrimidal and crystallize in the hexagonal space group P3(1)21 (or P3(2)21) with one dimer per asymmetric unit. The unit cell dimensions are a = b = 170.5 A, c = 161.7 A. The crystals diffract to 3 A resolution.

Citing Articles

Botulinum neurotoxin structure, engineering, and novel cellular trafficking and targeting.

Singh B Neurotox Res. 2006; 9(2-3):73-92.

PMID: 16785103 DOI: 10.1007/BF03033925.


Mapping of the antibody-binding regions on botulinum neurotoxin H-chain domain 855-1296 with antitoxin antibodies from three host species.

Atassi M, Dolimbek B, Hayakari M, Middlebrook J, Whitney B, Oshima M J Protein Chem. 1996; 15(7):691-700.

PMID: 8968960 DOI: 10.1007/BF01886751.


Botulinum type A neurotoxin digested with pepsin yields 132, 97, 72, 45, 42, and 18 kD fragments.

Gimenez J, Dasgupta B J Protein Chem. 1993; 12(3):351-63.

PMID: 8397793 DOI: 10.1007/BF01028197.


Covalent structure of botulinum neurotoxin type A: location of sulfhydryl groups, and disulfide bridges and identification of C-termini of light and heavy chains.

Krieglstein K, Dasgupta B, Henschen A J Protein Chem. 1994; 13(1):49-57.

PMID: 8011071 DOI: 10.1007/BF01891992.