| Literature DB >> 11092945 |
K Niefind1, B Guerra, I Ermakowa, 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 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%.Entities:
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Year: 2000 PMID： 11092945 DOI： 10.1107/s0907444900013627
Source DB: PubMed Journal: Acta Crystallogr D Biol Crystallogr ISSN： 0907-4449