Open AccessExpression, purification and crystallization of a PCI domain from the COP9 signalosome subunit 7 (CSN7)
Author(s) -
Dessau Moshe,
Chamovitz Daniel A.,
Hirsch Joel A.
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106041959
Subject(s) - crystallization , cop9 signalosome , orthorhombic crystal system , protein subunit , crystallography , materials science , polyethylene glycol , chemistry , biochemistry , crystal structure , organic chemistry , peptide hydrolases , gene , protease , enzyme
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 C 222 1 , with unit‐cell parameters a = 57.2, b = 86.2, c = 72.6 Å and a diffraction limit of 2.06 Å.