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

Cloning, purification and crystallization of Bacillus anthracis class C acid phosphatase

Buy Article:

$52.00 + tax (Refund Policy)

Cloning, expression, purification and crystallization studies of a recombinant class C acid phosphatase from the Category A pathogen Bacillus anthracis are reported. Large diffraction‐quality crystals were grown in the presence of HEPES and Jeffamine ED‐2001 at pH 7.0. The crystals belong to space group P212121, with unit‐cell parameters a = 53.4, b = 90.1, c = 104.2 Å. The asymmetric unit is predicted to contain two protein molecules with a solvent content of 38%. Two native data sets were collected from the same crystal before and after flash‐annealing. The first data set had a mosaicity of 1.6° and a high‐resolution limit of 1.8 Å. After flash‐annealing, the apparent mosaicity decreased to 0.9° and the high‐resolution limit of usable data increased to 1.6 Å. This crystal form is currently being used to determine the structure of B. anthracis class C acid phosphatase with experimental phasing techniques.
No References
No Citations
No Supplementary Data
No Article Media
No Metrics

Keywords: Bacillus anthracis; class C acid phosphatases; flash‐annealing

Document Type: Research Article

Publication date: July 1, 2006

  • 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