Skip to main content
padlock icon - secure page this page is secure

High‐level expression, purification, crystallization and preliminary X‐ray crystallographic studies of the receptor‐binding domain of botulinum neurotoxin serotype D

Buy Article:

$52.00 + tax (Refund Policy)

Botulinum neurotoxins (BoNTs) are highly toxic proteins for humans and animals that are responsible for the deadly neuroparalytic disease botulism. Here, details of the expression and purification of the receptor‐binding domain (HCR) of BoNT/D in Escherichia coli are presented. Using a codon‐optimized cDNA, BoNT/D_HCR was expressed at a high level (150–200 mg per litre of culture) in the soluble fraction. Following a three‐step purification protocol, very pure (>98%) BoNT/D_HCR was obtained. The recombinant BoNT/D_HCR was crystallized and the crystals diffracted to 1.65 Å resolution. The crystals belonged to space group P212121, with unit‐cell parameters a = 60.8, b = 89.7, c = 93.9 Å. Preliminary crystallographic data analysis revealed the presence of one molecule in the asymmetric unit.
No References
No Citations
No Supplementary Data
No Article Media
No Metrics

Keywords: botulinum neurotoxin; codon optimization; receptor‐binding domain

Document Type: Research Article

Publication date: December 1, 2010

  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
X
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more