Crystallization and preliminary X-ray diffraction analysis of Wza outer-membrane lipoprotein from Escherichia coli serotype O9a:K30

Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):558-60. doi: 10.1107/S0907444903029494. Epub 2004 Feb 25.

Abstract

A novel integral membrane lipoprotein, Wza, from Escherichia coli serotype O9a:K30 has been purified and crystallized. Wza is required for the surface expression of the serotype K30 group 1 capsular polysaccharide of E. coli; closely related homologues are found in other bacteria that produce extracellular polysaccharides. The Wza crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 94.6, b = 215.5, c = 218.5 A. A data set to 3.0 A with 99.8% completeness and an R(merge) of 10.5% has been collected from a single crystal.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antigens, Bacterial / biosynthesis
  • Antigens, Surface / biosynthesis
  • Bacterial Outer Membrane Proteins / chemistry*
  • Bacterial Outer Membrane Proteins / metabolism
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli / enzymology*
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / metabolism
  • Polysaccharides / metabolism
  • Structural Homology, Protein

Substances

  • Antigens, Bacterial
  • Antigens, Surface
  • Bacterial Outer Membrane Proteins
  • Escherichia coli Proteins
  • K antigens
  • Polysaccharides
  • Wza protein, E coli