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

Yong-Qun Zhu, De-Yu Zhu, Hong-Xia Lu, Na Yang, Gen-Pei Li, Da-Cheng Wang
2005 Protein Peptide Letters  
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
more » ... 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.
doi:10.2174/0929866054864184 pmid:16305556 fatcat:n3qf6khyc5glfjwevhwaqgr4xm