Protein preparation, crystallization and preliminary X‐ray crystallographic analysis of SMU.961 protein from the caries pathogen Streptococcus mutans

Publisher: John Wiley & Sons Inc

E-ISSN: 1744-3091|63|10|882-883

ISSN: 1744-3091

Source: Acta Crystallographica Section F, Vol.63, Iss.10, 2007-10, pp. : 882-883

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Abstract

The smu.961 gene encodes a putative protein of 183 residues in Streptococcus mutans, a major pathogen in human dental caries. The gene was cloned into expression vector pET28a and expressed in a substantial quantity in Escherichia coli strain BL21 (DE3) with a His tag at its N‐terminus. The recombinant protein SMU.961 was purified to homogeneity in a two‐step procedure consisting of Ni2+‐chelating and size‐exclusion chromatography. Crystals suitable for X‐ray diffraction were obtained by the hanging‐drop vapour‐diffusion method and diffracted to 2.9 Å resolution at beamline I911‐3, MAX‐II‐lab, Sweden. The crystal belonged to space group C2, with unit‐cell parameters a = 98.62, b = 73.73, c = 184.73 Å, β = 98.82°.