Protein preparation, crystallization and preliminary X-ray crystallographic analysis of Smu.1475c from caries pathogen Streptococcus mutans

Biochim Biophys Acta. 2006 Feb;1764(2):324-6. doi: 10.1016/j.bbapap.2005.11.022. Epub 2005 Dec 28.

Abstract

The gene smu.1475c encodes a putative protein of 211 residues in Streptococcus mutans, a primary pathogen for human dental caries. In this work, smu.1475c was cloned into pET28a and expressed in good amount from the E. coli strain BL21 (DE3). Smu.1475c protein was purified to homogeneity in a two-step procedure of Ni2+ chelating and size exclusion chromatography. Crystals were obtained by hanging-drop vapor-diffusion method and diffracted to 2.7 angstroms resolution. The crystal belongs to orthorhombic space group P2(1)2(1)2(1) with cell dimension of a = 68.3 angstroms, b = 105.9 angstroms, c = 136.2 angstroms. The asymmetric unit is expected to contain four molecules with solvent content of 49.4%.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / biosynthesis*
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Cloning, Molecular
  • Crystallization
  • Crystallography, X-Ray
  • Dental Caries / microbiology
  • Molecular Sequence Data
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Streptococcus mutans / metabolism*

Substances

  • Bacterial Proteins
  • Recombinant Proteins