Crystallization and preliminary X-ray analysis of the unliganded recombinant catalytic subunit of cAMP-dependent protein kinase

Acta Crystallogr D Biol Crystallogr. 1998 Nov 1;54(Pt 6 Pt 2):1401-4. doi: 10.1107/s0907444998005770.

Abstract

X-ray diffraction-quality crystals of the unliganded mouse recombinant catalytic subunit of cAMP-dependent protein kinase were grown by the hanging-drop vapour-diffusion technique using 2-methyl-2,4-pentanediol as precipitant. The crystals belong to the monoclinic space group P21 with unit-cell parameters a = 48.9, b = 147.4, c = 54.2 A, beta = 110.2 degrees. A data set to 3.0 A resolution with 92% completeness has been collected using synchrotron radiation. The unit cell contains four molecules of molecular weight 40 kDa with a corresponding volume solvent content of 45%.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Catalytic Domain
  • Crystallization
  • Crystallography, X-Ray
  • Cyclic AMP-Dependent Protein Kinases / chemistry*
  • Cyclic AMP-Dependent Protein Kinases / isolation & purification
  • Escherichia coli
  • Mice
  • Myocardium / enzymology
  • Protein Conformation
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / isolation & purification
  • Swine

Substances

  • Recombinant Fusion Proteins
  • Cyclic AMP-Dependent Protein Kinases