Abstract
The three-dimensional crystal structure of the triple-point mutant of the catalytic subunit of human protein kinase CK2alpha has been determined at 2.4 A resolution. Microcrystals of mutant CK2 catalytic subunit were obtained by a protein-crystallization method based on thin-film nanotechnology. These microcrystals (of about 20 micro m in diameter) were used for diffraction data collection by means of the microfocus beamline at the ESRF synchrotron. A comparison between the human protein kinase CK2alpha and the corresponding enzyme from a lower organism (Zea mays) is made.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Base Sequence
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Binding Sites
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Casein Kinase II
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Catalytic Domain
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Crystallization / methods
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Crystallography, X-Ray
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Humans
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Models, Molecular
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Molecular Sequence Data
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Point Mutation
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Protein Conformation
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Protein Serine-Threonine Kinases / chemistry*
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Protein Serine-Threonine Kinases / genetics
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Static Electricity
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Zea mays / enzymology
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Zea mays / genetics
Substances
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Recombinant Proteins
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Casein Kinase II
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Protein Serine-Threonine Kinases