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1: Acta Crystallogr D Biol Crystallogr. 2000 Dec;56(Pt 12):1680-4.Click here to read Links

Crystallization and preliminary characterization of crystals of human protein kinase CK2.

Niefind K, Guerra B, Ermakowa I, Issinger OG.

Universität zu Köln, Institut für Biochemie, Zülpicher Strasse 47, D-50674 Köln, Germany. karsten.niefind@uni-koeln.de

The heterotetrameric recombinant holoenzyme of human protein kinase CK2 was purified to homogeneity. It degraded spontaneously to a stable and fully active state in which the catalytic subunit was about 5 kDa smaller than the wild type. The degraded enzyme was crystallized using polyethylene glycol 3350 as precipitant. The crystals belong to the hexagonal space group P6(3). They have unit-cell parameters a = b = 176.0, c = 93.6 A and diffract X-rays to at least 3.5 A resolution. The calculated crystal packing parameter is V(M) = 3.22 A(3) Da(-1), suggesting that one CK2 tetramer is contained in the asymmetric unit and that the solvent content of the unit cell is 62%.

PMID: 11092945 [PubMed - indexed for MEDLINE]

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