Crystallization and preliminary X-ray analysis of the cAMP-dependent protein kinase catalytic subunit from Saccharomyces cerevisiae

Kuret, J., Pflugrath, J. W. (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)

URL: http://www.ncbi.nlm.nih.gov/pubmed/1931981
DOI: 10.1021/bi00107a031

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
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 Deposited: 13 Jan 2016 16:40
Last Modified: 13 Jan 2016 16:47
Related URLs:
URI: http://repository.cshl.edu/id/eprint/32063

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