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.

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 P2(1), with unit-cell parameters ...
a = 60.38, b = 100.22, c = 72.20 A, beta = 94.70 degrees and with three Nas6-Rpt3C molecules per asymmetric unit. The crystal diffracted to beyond 2.2 A resolution using synchrotron radiation.
Mesh Terms:
Adenosine Triphosphatases, Crystallization, Crystallography, X-Ray, DNA-Binding Proteins, Humans, Proteasome Endopeptidase Complex, Protein Subunits, Proto-Oncogene Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, X-Ray Diffraction
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
Date: Mar. 01, 2007
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