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. 1998 Jan 1;54(Pt 1):143-5.
doi: 10.1107/s0907444997010184.

Expression, purification and crystallization of the catalytic subunit of protein kinase CK2 from Zea mays

B Guerra  1 , K Niefind, L A Pinna, D Schomburg, O G Issinger
Affiliations

Expression, purification and crystallization of the catalytic subunit of protein kinase CK2 from Zea mays

B Guerra et al. Acta Crystallogr D Biol Crystallogr. .

Abstract

The catalytic (alpha) subunit of protein kinase CK2 (CK2alpha) was originally cloned and overexpressed in the Escherichia coli strain pT7-7/BL21(DE3). The protein has been purified to homogeneity and crystallized. The crystals belong to the monoclinic space group C2, they have unit-cell parameters a = 142.6, b = 61.3, c = 45.6 A, beta = 103.3 degrees and diffract X-rays to at least 2.0 A resolution. The calculated crystal packing parameter is Vm = 2.47 A3 Da-1 suggesting that one CK2alpha molecule is contained in the asymmetric unit and that the solvent content of the unit cell is 50%.

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