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Purification and preliminary crystallographic studies of CutC, a novel copper homeostasis protein from Shigella
Yong-Qun Zhu1, De-Yu Zhu, Hong-Xia Lu
1Center for Structural and Molecular Biology, Institute of biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang district, Beijing 100101, People's Republic of China.
Abstract:
CutC is a novel copper homeostasis protein containing 248 amino acids. Here we report the cloning, expression, purification, crystallization and preliminary X-ray crystallographic studies of CutC from Shigella flexneri 2a. Purification of CutC and its selenomethionine (SeMet) derivate were done using immobilized metal ion affinity chromatography, size-exclusion and ion-exchange chromatography. The purified proteins were crystallized using the hanging drop vapor diffusion method. The diffraction data for the native and SeMet CutC, respectively, have been collected with resolution of 1.7 A and 2.1 A. They belong to the space group C2221 and similar cell dimension. The native protein crystals have cell parameters: a=75.3267, b=97.6718, c=132.6910.
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