Abstract
The gene smu.1475c encodes a putative protein of 211 residues in Streptococcus mutans, a primary pathogen for human dental caries. In this work, smu.1475c was cloned into pET28a and expressed in good amount from the E. coli strain BL21 (DE3). Smu.1475c protein was purified to homogeneity in a two-step procedure of Ni 2+ chelating and size exclusion chromatography. Crystals were obtained by hanging-drop vapor-diffusion method and diffracted to 2.7 Å resolution. The crystal belongs to orthorhombic space group P2 12 12 1 with cell dimension of a = 68.3 Å, b = 105.9 Å, c = 136.2 Å. The asymmetric unit is expected to contain four molecules with solvent content of 49.4%.
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