Crystallization and preliminary X-ray crystallographic analysis of the hexameric human p97/VCP ND1 fragment in complex with the UBX domain of human FAF1.

The UBX domain of Fas-associated factor 1 (FAF1) binds to the N domain of p97/VCP, a multi-functional hexameric ATPase, and FAF1 thus inhibits the proteasome-mediated protein-degradation process assisted by p97/VCP. Here, crystallization of the hexameric p97/VCP ND1 fragment in complex with the FAF1 UBX domain is reported. Wild-type p97/VCP ND1 ...
in complex with FAF1 UBX crystallized into very thin sheet-shaped crystals which turned out to be of poor diffraction quality. Therefore, in order to acquire a better diffraction-quality crystal, three mutants of p97/VCP ND1 were generated based on the surface-entropy reduction method. Of these, a triple mutant was the most successful in producing diffraction-quality crystals suitable for subsequent structural analysis. X-ray data were collected to 3.60 A resolution and the crystals belonged to space group I222, with unit-cell parameters a = 166.28, b = 170.04, c = 255.99 A. The Matthews coefficient and solvent content were estimated to be 5.78 A(3) Da(-1) and 78.72%, respectively.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Adenosine Triphosphatases, Cell Cycle Proteins, Crystallography, X-Ray, Humans, Protein Multimerization
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
Date: Oct. 01, 2011
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