Purification and Preliminary Crystallographic Studies of CutC, a Novel Copper Homeostasis Protein from Shigella flexneri

Title: Purification and Preliminary Crystallographic Studies of CutC, a Novel Copper Homeostasis Protein from Shigella flexneri

Volume: 12 Issue: 8

Author(s): Yong-Qun Zhu, De-Yu Zhu, Hong-Xia Lu, Na Yang, Gen-Pei Li and Da-Cheng Wang

Affiliation:

Keywords: cutc, copper homeostasis protein, purification, crystallization, preliminary crystallographic studies, shigella flexneri

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 Å and 2.1 Å. 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.

Cite this article as:

Zhu Yong-Qun, Zhu De-Yu, Lu Hong-Xia, Yang Na, Li Gen-Pei and Wang Da-Cheng, Purification and Preliminary Crystallographic Studies of CutC, a Novel Copper Homeostasis Protein from Shigella flexneri, Protein & Peptide Letters 2005; 12 (8) . https://dx.doi.org/10.2174/0929866054864184