Expression, purification and X-ray characterization of residues 18-230 from the pneumococcal histidine triad protein A (PhtA) from Streptococcus pneumoniae

Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):926-8. doi: 10.1107/S0907444904004573. Epub 2004 Apr 21.

Abstract

A fragment of the Streptococcus pneumoniae PhtA gene product (residues 18-230) was cloned and overexpressed in Escherichia coli. The purified protein was crystallized using the sitting-drop vapour-diffusion technique. Crystals belong to the monoclinic space group C2, with unit-cell parameters a = 62.19, b = 35.9, c = 72.54 A, beta = 90.01 degrees. The crystals diffract X-rays to beyond 1.2 A resolution.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli / genetics
  • Hydrolases / chemistry*
  • Hydrolases / genetics
  • Hydrolases / isolation & purification*
  • Peptide Fragments / chemistry
  • Peptide Fragments / genetics
  • Peptide Fragments / isolation & purification
  • Protein Conformation
  • Recombinant Proteins / genetics
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Streptococcus pneumoniae / chemistry*

Substances

  • Peptide Fragments
  • Recombinant Proteins
  • histidine triad protein
  • Hydrolases