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

Bushell, S.R.; Lou, H.; Wallat, G.D.; Beis, K.; Whitfield, C.; Naismith, J.H.

doi:10.1107/S1744309110040546

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 2
Purification of native Wzi-His₆. (a) Elution profile of native Wzi-His₆ (blue line) on size-exclusion chromatography using a Superdex 200 10/300 column. The elution was standardized using a mixture containing (1) thyroglobulin (670 kDa), (2) γ-globulin (158 kDa), (3) ovalbumin (44 kDa), (4) myoglobin (17 kDa) and (5) vitamin B₁₂ (1350 Da) (red line). The protein aggregate peak (marked with an asterisk) represents the void volume of the column. (b) SDS–PAGE analysis of peak fractions from SEC purification, showing the homogeneity of Wzi-His₆ immediately prior to crystallization. The protein runs to its true size of 52 kDa upon boiling.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 66| Part 12| December 2010| Pages 1621-1625

https://doi.org/10.1107/S1744309110040546

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