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

Moshe Dessau, Daniel A. Chamovitz, Joel A. Hirsch

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

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 C2221, with unit-cell parameters a = 57.2, b = 86.2, c = 72.6 Å and a diffraction limit of 2.06 Å.

Original languageEnglish
Pages (from-to)1138-1140
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume62
Issue number11
DOIs
StatePublished - 1 Nov 2006
Externally publishedYes

Keywords

  • COP9 signalosome
  • PCI and MPN motifs
  • Proteasome

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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