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

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

Journal Name: Protein & Peptide Letters

Volume 14 , Issue 5 , 2007


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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.

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

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Article Details

VOLUME: 14
ISSUE: 5
Year: 2007
Published on: 01 March, 2012
Page: [503 - 504]
Pages: 2
DOI: 10.2174/092986607780782759
Price: $65

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