Protein preparation and preliminary X-ray crystallographic analysis of a putative glucosamine 6-phosphate deaminase from Streptococcus mutants

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Sep 1;63(Pt 9):809-11. doi: 10.1107/S1744309107040304. Epub 2007 Aug 31.

Abstract

The SMU.636 protein from Streptococcus mutans is a putative glucosamine 6-phosphate deaminase with 233 residues. The smu.636 gene was PCR-amplified from S. mutans genomic DNA and cloned into the expression vector pET-28a(+). The resultant His-tagged fusion protein was expressed in Escherichia coli and purified to homogeneity in two steps. Crystals of the fusion protein were obtained by the hanging-drop vapour-diffusion method. The crystals diffracted to 2.4 A resolution and belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 53.83, b = 82.13, c = 134.70 A.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aldose-Ketose Isomerases / chemistry*
  • Aldose-Ketose Isomerases / genetics
  • Aldose-Ketose Isomerases / isolation & purification
  • Amino Acid Sequence
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / isolation & purification
  • Conserved Sequence
  • Crystallization
  • Crystallography, X-Ray
  • Molecular Sequence Data
  • Polymerase Chain Reaction
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Sequence Alignment
  • Streptococcus mutans / enzymology*

Substances

  • Bacterial Proteins
  • Recombinant Proteins
  • glucosamine-6-phosphate isomerase
  • Aldose-Ketose Isomerases