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The catalytic subunit of phosphorylase kinase is composed of a kinase catalytic core domain (residues 1 to 298), which has a 33% identity with the kinase core of the cyclic AMP-dependent protein kinase, and a C-terminal calmodulin binding domain. The kinase domain of the catalytic subunit has been expressed in Escherichia coli, purified and crystallised in the presence of ATP and magnesium from 5% (w/v) polyethylene glycol 8000, 10% (v/v) glycerol, 50 mM Hepes/NaOH (pH 6.9). A three-fold excess of magnesium to ATP was used for crystal growth. The inclusion of glycerol in the crystallization medium produced a marked reduction in mosaic spread of the diffraction spots from greater than 1 degree to 0.3 degree. The crystals are orthorhombic, space group P2(1)2(1)2(1) with unit cell dimensions a = 47.1 A, b = 69.1 A, c = 112.9 A and one molecule per asymmetric unit. Data to 3 A resolution have been collected and structure determination is in progress.

Original publication

DOI

10.1006/jmbi.1994.0092

Type

Journal article

Journal

J Mol Biol

Publication Date

24/02/1995

Volume

246

Pages

374 - 381

Keywords

Animals, Catalysis, Chromatography, Affinity, Cloning, Molecular, Crystallization, Crystallography, X-Ray, Electrophoresis, Polyacrylamide Gel, Escherichia coli, Muscle, Skeletal, Mutagenesis, Site-Directed, Phosphorylase Kinase, Rabbits