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

Purification, crystallization and preliminary crystallographic analysis of SMU.1108c protein from Streptococcus mutans

Buy Article:

$52.00 + tax (Refund Policy)

Streptococcus mutans SMU.1108c (KEGG database) encodes a functionally uncharacterized protein consisting of 270 amino‐acid residues. This protein is predicted to have a haloacid dehalogenase hydrolase‐like domain and is a homologue of haloacid dehalogenase phosphatases that catalyze phosphoryl‐transfer reactions. In this work, SMU.1108c was cloned into the pET28a vector and overexpressed in Escherichia coli strain BL21 (DE3). The protein was purified to homogeneity and crystallized using the sitting‐drop vapour‐diffusion method. The best crystal diffracted to 2.0 Å resolution and belonged to space group C2, with unit‐cell parameters a = 77.1, b = 80.2, c = 47.9 Å, β = 99.5°.
No References
No Citations
No Supplementary Data
No Article Media
No Metrics

Keywords: SMU.1108c; Streptococcus mutans; haloacid dehalogenase superfamily

Document Type: Research Article

Affiliations: The National Laboratory of Protein Engineering and Plant Genetic Engineering, School of Life Sciences, Peking University, Beijing 100871, People's Republic of China

Publication date: January 1, 2011

  • 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