Niefind K, Guerra B, Ermakowa I, Issinger O G
Universität zu Köln, Institut für Biochemie, Zülpicher Strasse 47, D-50674 Köln, Germany.
Acta Crystallogr D Biol Crystallogr. 2000 Dec;56(Pt 12):1680-4. doi: 10.1107/s0907444900013627.
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%.
人蛋白激酶CK2的异源四聚体重组全酶被纯化至同质。它会自发降解为一种稳定且完全有活性的状态，其中催化亚基比野生型小约5 kDa。使用聚乙二醇3350作为沉淀剂使降解后的酶结晶。晶体属于六方空间群P6(3)。它们的晶胞参数为a = b = 176.0，c = 93.6 Å，并且能将X射线衍射至至少3.5 Å的分辨率。计算得到的晶体堆积参数为V(M) = 3.22 Å(3) Da(-1)，这表明不对称单元中包含一个CK2四聚体，且晶胞的溶剂含量为62%。
