Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 63, Part 3 (March 2007)

crystallization communications

Acta Cryst. (2007). F63, 190-192 [ doi:10.1107/S1744309107004848 ]

Purification, crystallization and preliminary X-ray diffraction analysis of the non-ATPase subunit Nas6 in complex with the ATPase subunit Rpt3 of the 26S proteasome from Saccharomyces cerevisiae

Y. Nakamura, T. Umehara, A. Tanaka, M. Horikoshi, B. Padmanabhan and S. Yokoyama

Abstract: The non-ATPase subunit Nas6, which is the human orthologue of gankyrin, was co-expressed with the C-terminal domain of the ATPase subunit Rpt3 of the yeast 26S proteasome in Escherichia coli, purified to near-homogeneity and crystallized using the hanging-drop vapour-diffusion method. The protein crystallized in space group P2₁, with unit-cell parameters a = 60.38, b = 100.22, c = 72.20 Å, [beta] = 94.70° and with three Nas6-Rpt3C molecules per asymmetric unit. The crystal diffracted to beyond 2.2 Å resolution using synchrotron radiation.

Keywords: Nas6; gankyrin; oncoproteins; Rpt3; proteasome; protein degradation; ubiquitin.