Expression, purification and crystallization of the catalytic subunit of protein kinase CK2 from Zea mays.
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%.
Guerra
B
B
Odense Universitet, Biokemisk Institut, Campusvej 55, DK-5230 Odense, Denmark.
Niefind
K
K
Pinna
L A
LA
Schomburg
D
D
Issinger
O G
OG
D047390:Casein Kinase II; D020134:Catalytic Domain; D003460:Crystallization; D018360:Crystallography, X-Ray; D017346:Protein Serine-Threonine Kinases / Q000096:biosynthesis* / Q000737:chemistry / Q000302:isolation & purification
D047390:Casein Kinase II; D017346:Protein Serine-Threonine Kinases