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To contribute to the molecular understanding of the function of a tandem-type universal stress protein, UspE from E. coli was overexpressed and crystals of the recombinant protein were obtained using sitting-drop vapour diffusion. A diffraction data set was collected to a resolution of 3.2 Å.

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In this study, the crystal structure of a DsbE or DsbF homologue protein from Corynebacterium diphtheriae has been determined, which revealed a thioredoxin-like domain with a typical CXXC active site.
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