Expression, purification and crystallization of a PCI domain from the COP9 signalosome subunit 7 (CSN7)

Abstract

A core fragment of Arabidopsis thaliana COP9 signalosome (CSN) subunit 7 was expressed in Escherichia coli. The protein was purified to homogeneity and screened for crystallization. Crystallization conditions were refined using the sitting-drop vapour-diffusion method. Crystals were obtained using polyethylene glycol 8000 as a precipitant and have a thick rod-like morphology. Their crystallographic symmetry is orthorhombic, space group C222(1), with unit-cell parameters a = 57.2, b = 86.2, c = 72.6 A and a diffraction limit of 2.06 A.