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

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

Document Type: Research Article

DOI: https://doi.org/10.2174/092986607780782759

Publication date: 2007-05-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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