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

Bushell, Simon R; Lou, Hubing; Wallat, Gregor D; Beis, Konstantinos; Whitfield, Chris; Naismith, James H.
Acta Crystallogr Sect F Struct Biol Cryst Commun; 66(Pt 12): 1621-5, 2010 Dec 01.
Artigo em Inglês | MEDLINE | ID: mdl-21139210
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 ß-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 Šresolution. 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, α=ß=γ=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 Šresolution. Data processing shows that the variant crystal has similar unit-cell parameters to the native crystal.
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