Crystallization and Preliminary X-Ray Crystallographic Studies of SMU.134 Protein from Caries Pathogen Streptococcus mutans

Title: Crystallization and Preliminary X-Ray Crystallographic Studies of SMU.134 Protein from Caries Pathogen Streptococcus mutans

Volume: 14 Issue: 5

Author(s): Hua Li, Lan-Fen Li, Xiao-Dong Su, Xiaojun Zhao and Yu-He Liang

Affiliation:

Keywords: polymerase chain reaction, open reading frames, clostridium beijerincki, sds-page, luria-bertani

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 pET28?? 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 Ni2+ chelating and size exclusion chromatography. Crystals suitable for X-ray diffraction were obtained by hanging-drop vapor diffusion method and diffracted to 2.6 Å. The crystal belonged to space group P212121, with unit-cell parameters a=55.03 Å, b=80.84 Å, c=107.96 Å.

Cite this article as:

Li Hua, Li Lan-Fen, Su Xiao-Dong, Zhao Xiaojun and Liang Yu-He, Crystallization and Preliminary X-Ray Crystallographic Studies of SMU.134 Protein from Caries Pathogen Streptococcus mutans, Protein & Peptide Letters 2007; 14(5) . https://dx.doi.org/10.2174/092986607780782759