Abstract

Human CDK6 plays an important role in controlling entry into the eukaryotic cell cycle. An activated complex of human CDK6 with a viral cyclin from herpesvirus saimiri was purified to homogeneity and crystallized using polyethylene glycol 3350 as precipitant. Crystallization was critically dependent on a narrow range of calcium acetate concentration and the presence of sulfo-betaine 201 as additive. Crystals belong to the hexagonal space group P6(1)22 or P6(5)22, with unit-cell parameters a = b = 70.14, c = 448.77 A, gamma = 120 degrees, and diffract X-rays to at least 3.1 A resolution.

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