Crystallization and preliminary X-ray analysis of the cAMP-dependent protein kinase catalytic subunit from Saccharomyces cerevisiae.
A truncated variant of TPK1, the yeast cAMP-dependent protein kinase catalytic subunit, was overexpressed in an engineered strain of Saccharomyces cerevisiae, purified by liquid chromatography, and crystallized from solutions of 2-propanol and magnesium at alkaline pH. The crystals are hexagonal dipyramids, space group P6(1)22 (P6(5)22), with unit-cell parameters a = b = 61 A, c = 320 A. Large single crystals suitable for diffraction analysis are obtainable by microseeding, and diffract beyond 2.8-A resolution. Crystal density measurements reveal 12 kinase monomers per unit cell with a single kinase monomer per asymmetric unit.
Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724.
J
J
Kuret
J W
JW
Pflugrath
D001483:Base Sequence; D002384:Catalysis; D002853:Chromatography, Liquid; D003460:Crystallization; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D011494:Protein Kinases / Q000737:chemistry*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D014961:X-Ray Diffraction
D011494:Protein Kinases