Preliminary X-ray diffraction analysis of YcdB from Escherichia coli: a novel haem-containing and Tat-­secreted periplasmic protein with a potential role in iron transport

Cartron, M.L.; Mitchell, S.A.; Woodhall, M.R.; Andrews, S.C.; Watson, K.A.

doi:10.1107/S174430910604509X

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 1
Purification of apo-(His)₆YcdB. (a) SDS–PAGE (12% acrylamide) of samples at different stages of apo-(His)₆YcdB purification from the (His)₆YcdB overexpressing strain. MWM, molecular-weight markers (kDa); lane 1, soluble crude extract following cell lysis and centrifugation; lane 2, apo-(His)₆YcdB after Ni²⁺-affinity chromatography; lane 3, apo-(His)₆YcdB following anion-exchange chromatography. Approximately 50, 20 and 5 µg of protein were loaded in lanes 1, 2 and 3, respectively. (b) Elution profile of overexpressed (His)₆YcdB during Ni²⁺-affinity chromatography. The concentration of imidazole applied to the column is indicated, as are the elution peaks corresponding to the apo and holo forms of (His)₆YcdB.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 63| Part 1| December 2007| Pages 37-41

doi:10.1107/S174430910604509X

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