Crystallization and preliminary crystallographic analysis of recombinant immunoglobulin G-binding protein from Streptococcus suis

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Aug 1;64(Pt 8):757-9. doi: 10.1107/S1744309108020149. Epub 2008 Jul 31.

Abstract

Streptococcus suis, an important zoonotic pathogen, expresses immunoglobulin G-binding protein, which is thought to be helpful to the organism in eluding the host defence system. Recombinant IgG-binding protein expressed in Escherichia coli has been crystallized using the hanging-drop vapour-diffusion method. The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 38.98, b = 43.94, c = 78.17 A and one molecule in the asymmetric unit. Diffraction data were collected to 2.60 A resolution.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / isolation & purification
  • Cloning, Molecular
  • Crystallization
  • Crystallography, X-Ray
  • Electrophoresis, Polyacrylamide Gel
  • Protein Conformation
  • Recombinant Proteins / chemistry
  • Streptococcus suis / chemistry*

Substances

  • Bacterial Proteins
  • IgG Fc-binding protein, Streptococcus
  • Recombinant Proteins