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Crystallization and preliminary diffraction analysis of Wzi, a member of the capsule export and assembly pathway in Escherichia coli

DOI: 10.1107/S1744309110040546 DOI Help

Authors: Simon R. Bushell (University of St Andrews) , Hubing Lou (University of St Andrews) , Gregor Wallat (University of St Andrews) , Konstantinos Beis (Diamond Light Source) , Chris Whitfield (Centre for Biomolecular Sciences, The University of St. Andrews) , James Naismith (Center for Biomolecular Sciences, University of St. Andrews)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology And Crystallization Communications , VOL 66 (12) , PAGES 1621-1625

State: Published (Approved)
Published: December 2010

Abstract: External polysaccharide capsules provide a physical barrier that is employed by many species of bacteria for the purposes of host evasion and persistence. Wzi is a 53 kDa outer membrane [beta]-barrel protein that is thought to play a role in the attachment of group 1 capsular polysaccharides to the cell surface. The purification and crystallization of an Escherichia coli homologue of Wzi is reported and diffraction data from native and selenomethionine-incorporated protein crystals are presented. Crystals of C-terminally His6-tagged Wzi diffracted to 2.8 Å resolution. Data processing showed that the crystals belonged to the orthorhombic space group C222, with unit-cell parameters a = 128.8, b = 152.8, c = 94.4 Å, [alpha] = [beta] = [gamma] = 90°. A His-tagged selenomethionine-containing variant of Wzi has also been crystallized in the same space group and diffraction data have been recorded to 3.8 Å resolution. Data processing shows that the variant crystal has similar unit-cell parameters to the native crystal.

Journal Keywords: Wzi; polysaccharide capsules; Escherichia coli

Subject Areas: Biology and Bio-materials


Instruments: I24-Microfocus Macromolecular Crystallography

Other Facilities: ESRF