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

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, ?=99.5°.

SUBMITTER: Feng MJ

PROVIDER: S-EPMC3079977 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature

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

Feng Ming Jing MJ Fu Tian Min TM Liu Xiang X Li Lan Fen LF

Acta crystallographica. Section F, Structural biology and crystallization communications 20101222 Pt 1

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 sit ...[more]

PMID: 21206029

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