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Updated: Jun 5, 2026
Purification of a High Molecular Mass Protein in Streptococcus mutans
Published on: September 14, 2019
Purification, crystallization and preliminary crystallographic analysis of SMU.1108c protein from Streptococcus
Ming Jing Feng1, Tian Min Fu, Xiang Liu
1The National Laboratory of Protein Engineering and Plant Genetic Engineering, School of Life Sciences, Peking University, Beijing 100871, People's Republic of China.
Abstract:
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°.
