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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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The tripartite motif-containing protein 2 (TRIM2) functions as an E3 ubiquitin ligase. The crystal structure of the NHL domain of TRIM2, which belonged to space group P21, with unit-cell parameters a = 43.6, b = 76.4, c = 107.4 Å, α = 90.0, β = 94.0 and γ = 90.0° has been determined.
Keywords: TRIM2; NHL domain.
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