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Updated: Aug 26, 2026

From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
Published on: July 4, 2016
Crystallization and preliminary X-ray diffraction analysis of Wza outer-membrane lipoprotein from Escherichia coli
Konstantinos Beis1, Jutta Nesper, Chris Whitfield
1Centre for Biomolecular Sciences, University of St Andrews, North Haugh, St Andrews, Fife KY16 9ST, Scotland.
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.

