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Updated: Jul 14, 2026

Purification of a High Molecular Mass Protein in Streptococcus mutans
Published on: September 14, 2019
Crystallization and preliminary X-ray crystallographic studies of SMU.134 protein from caries pathogen Streptococcus
Hua Li1, Lan-Fen Li, Xiao-Dong Su
1Institute for Nanobiomedical Technology and Membrane Biology, West China Hospital, Sichuan University, Chengdu 610065, Sichuan, China.
Abstract:
The smu.134 gene encodes a putative transcriptional regulator of 217 residues in Streptococcus mutans, a major pathogen for human dental caries. The gene was cloned into expression vector pET28alpha and expressed in soluble form in E. coli strain BL21 (DE3) with a His tag at its N-terminus. The recombinant protein SMU.134 was purified to homogeneity in a two step procedure of Ni(2+ ) chelating and size exclusion chromatography. Crystals suitable for X-ray diffraction were obtained by hanging-drop vapor diffusion method and diffracted to 2.6 A;. The crystal belonged to space group P2(1)2(1)2(1), with unit-cell parameters a=55.03 A, b=80.84 A, c=107.96 A.
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