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  • Title: Preliminary X-ray crystallographic analysis of SMU.2055 protein from the caries pathogen Streptococcus mutans.
    Author: Zhao WH, Zhan XR, Gao XZ, Liu X, Zhang YF, Lin J, Li LF, Wei SC, Su XD.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2010 May 01; 66(Pt 5):530-3. PubMed ID: 20445252.
    Abstract:
    The SMU.2055 gene from the major caries pathogen Streptococcus mutans is annotated as a putative acetyltransferase with 163 amino-acid residues. In order to identify its function via structural studies, the SMU.2055 gene was cloned into the expression vector pET28a. Native and SeMet-labelled SMU.2055 proteins with a His(6) tag at the N-terminus were expressed at a high level in Escherichia coli strain BL21 (DE3) and purified to homogeneity by Ni(2+)-chelating affinity chromatography. Diffraction-quality crystals of SeMet-labelled SMU.2055 were obtained using the sitting-drop vapour-diffusion method and diffracted to a resolution of 2.5 A on beamline BL17A at the Photon Factory, Tsukuba, Japan. The crystals belong to the orthorhombic space group C222(1), with unit-cell parameters a = 92.0, b = 95.0, c = 192.2 A. The asymmetric unit contained four molecules, with a solvent content of 57.1%.
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