Kuret, J., Pflugrath, J. W. (October 1991) Crystallization and preliminary X-ray analysis of the cAMP-dependent protein kinase catalytic subunit from Saccharomyces cerevisiae. Biochemistry, 30 (43). pp. 10595-600. ISSN 0006-2960 (Print)0006-2960 (Linking)
Abstract
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.
Item Type: | Paper |
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Uncontrolled Keywords: | Base Sequence Catalysis Chromatography, Liquid Crystallization Electrophoresis, Polyacrylamide Gel Molecular Sequence Data Protein Kinases/*chemistry Saccharomyces cerevisiae/*enzymology X-Ray Diffraction |
Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > transcription factor > Cyclic AMP bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > kinase Investigative techniques and equipment > x ray crystallography organism description > yeast |
CSHL Authors: | |
Communities: | CSHL labs > Stillman lab |
Depositing User: | Matt Covey |
Date: | 29 October 1991 |
Date Deposited: | 13 Jan 2016 16:40 |
Last Modified: | 13 Jan 2016 16:47 |
Related URLs: | |
URI: | https://repository.cshl.edu/id/eprint/32063 |
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