Expression, purification and crystallization of a PCI domain from the COP9 signalosome subunit 7 (CSN7).
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.
Dessau
Moshe
M
Department of Biochemistry, Faculty of Life Sciences, Tel Aviv University, Ramat Aviv 69978, Israel.
Chamovitz
Daniel A
DA
Hirsch
Joel A
JA
D017360:Arabidopsis / Q000201:enzymology; D029681:Arabidopsis Proteins / Q000737:chemistry / Q000302:isolation & purification; D000075686:COP9 Signalosome Complex; D018360:Crystallography, X-Ray; D018076:DNA, Complementary; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D046912:Multiprotein Complexes / Q000737:chemistry*; D010447:Peptide Hydrolases / Q000737:chemistry*; D016133:Polymerase Chain Reaction; D021122:Protein Subunits / Q000737:chemistry / Q000302:isolation & purification*
D029681:Arabidopsis Proteins; D018076:DNA, Complementary; D046912:Multiprotein Complexes; D021122:Protein Subunits; D010447:Peptide Hydrolases; D000075686:COP9 Signalosome Complex