Crystallization and preliminary diffraction analysis of Wzi, a member of the capsule export and assembly pathway in Escherichia coli
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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 His(6)-tagged Wzi diffracted to 2.8 A 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 A, alpha = beta = gamma = 90 degrees. 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 A resolution. Data processing shows that the variant crystal has similar unit-cell parameters to the native crystal.
Bushell , S R , Lou , H , Wallat , G D , Beis , K , Whitfield , C & Naismith , J H 2010 , ' Crystallization and preliminary diffraction analysis of Wzi, a member of the capsule export and assembly pathway in Escherichia coli ' , Acta Crystallographica. Section F, Structural biology and crystallization communications , vol. 66 , no. 12 , pp. 1621-1625 . https://doi.org/10.1107/S1744309110040546
Acta Crystallographica. Section F, Structural biology and crystallization communications
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DescriptionSupported by a grant from The Wellcome Trust (081862/Z/06/Z)
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