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Purification and Preliminary Crystallographic Studies of CutC, a Novel Copper Homeostasis Protein from Shigella flexneri
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
doi:10.2174/0929866054864184
pmid:16305556
fatcat:n3qf6khyc5glfjwevhwaqgr4xm