Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase from Streptococcus suis serotype 2

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Nov 1;64(Pt 11):997-9. doi: 10.1107/S1744309108028340. Epub 2008 Oct 25.

Abstract

2-Keto-3-deoxy-6-phosphogluconate (KDPG) adolase from pathogenic Streptococcus suis serotype 2 was crystallized using the hanging-drop vapour-diffusion method at 291 K. X-ray diffraction data were collected to 2.8 A resolution. The crystal belonged to space group R32, with unit-cell parameters a = b = 126.4, c = 415.9 A, alpha = beta = 90, gamma = 120 degrees . Assuming the presence of six molecules in the asymmetric unit gave a V(M) value of 2.32 A(3) Da(-1) and a solvent content of 47.12%.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aldehyde-Lyases / chemistry*
  • Aldehyde-Lyases / genetics
  • Aldehyde-Lyases / isolation & purification*
  • Animals
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / isolation & purification*
  • Crystallography, X-Ray
  • Humans
  • Molecular Sequence Data
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Streptococcus suis / enzymology*
  • Swine
  • X-Ray Diffraction

Substances

  • Bacterial Proteins
  • Recombinant Proteins
  • Aldehyde-Lyases
  • phospho-2-keto-3-deoxy-gluconate aldolase