Open AccessPurification, crystallization and preliminary crystallographic analysis of SMU.1108c protein from Streptococcus mutans
Author(s) -
Feng MingJing,
Fu TianMin,
Liu Xiang,
Li LanFen
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911004457x
Subject(s) - protein crystallization , deinococcus radiodurans , chemistry , crystallization , streptococcus mutans , escherichia coli , crystallography , dehalogenase , biochemistry , biology , enzyme , bacteria , dna , gene , genetics , organic chemistry
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 C 2, with unit‐cell parameters a = 77.1, b = 80.2, c = 47.9 Å, β = 99.5°.