Acta Crystallographica Section D

Biological Crystallography

Volume 56, Part 12 (December 2000)

crystallization papers

Acta Cryst. (2000). D56, 1680-1684 [ doi:10.1107/S0907444900013627 ]

Crystallization and preliminary characterization of crystals of human protein kinase CK2

K. Niefind, B. Guerra, I. Ermakowa and O.-G. Issinger

Abstract: 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 P6₃. They have unit-cell parameters a = b = 176.0, c = 93.6 Å and diffract X-rays to at least 3.5 Å resolution. The calculated crystal packing parameter is V_M = 3.22 Å³ Da^-1, suggesting that one CK2 tetramer is contained in the asymmetric unit and that the solvent content of the unit cell is 62%.

Keywords: protein kinase CK2.