Crystallization and preliminary x-ray diffraction analysis of the regulatory subunit of human protein kinase CK2

Acta Crystallogr D Biol Crystallogr. 1999 Apr;55(Pt 4):895-7. doi: 10.1107/s0907444998016680.

Abstract

Protein kinase CK2 is a tetramer composed of two alpha catalytic subunits and two beta regulatory subunits. A C-terminal truncated form of the beta subunit has been overproduced in Escherichia coli and purified to homogeneity. Two crystal forms of the truncated protein which diffract to at least 2 A resolution have been obtained. Form I belongs to the monoclinic space group P21, with unit-cell parameters a = 49.9, b = 92.9, c = 53.7 A, beta = 96.3 degrees, and yields plate-like crystals. Form II belongs to the tetragonal space group P42212, with unit-cell parameters a = 132.19, b = 132.19, c = 63.79 A, and produces rod-shaped crystals. Both crystal forms have a functional dimer in the crystal asymmetric unit.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Casein Kinase II
  • Crystallization
  • Dimerization
  • Escherichia coli / enzymology
  • Escherichia coli / genetics
  • Humans
  • Macromolecular Substances
  • Protein Serine-Threonine Kinases / biosynthesis
  • Protein Serine-Threonine Kinases / chemistry*
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / isolation & purification
  • Solutions
  • X-Ray Diffraction

Substances

  • Macromolecular Substances
  • Solutions
  • Casein Kinase II
  • Protein Serine-Threonine Kinases