Open AccessCrystallization and preliminary diffraction analysis of Wzi, a member of the capsule export and assembly pathway in Escherichia coli
Author(s) -
Bushell Simon R.,
Lou Hubing,
Wallat Gregor D.,
Beis Konstantinos,
Whitfield Chris,
Naismith James H.
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110040546
Subject(s) - crystallization , escherichia coli , capsule , diffraction , crystallography , materials science , chemical engineering , chemistry , biology , biochemistry , physics , gene , optics , engineering , botany
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 β‐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 Å resolution. Data processing showed that the crystals belonged to the orthorhombic space group C 222, with unit‐cell parameters a = 128.8, b = 152.8, c = 94.4 Å, α = β = 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 Å resolution. Data processing shows that the variant crystal has similar unit‐cell parameters to the native crystal.