Abstract
Ligands interacting with Mycobacterium tuberculosis recombinant proteins were identified through use of the ability of Cibacron Blue F3GA dye to interact with nucleoside/nucleotide binding proteins, and the effects of these ligands on crystallization were examined. Co-crystallization with ligands enhanced crystallization and enabled X-ray diffraction data to be collected to a resolution of atleast 2.7 Å for 5 of 10 proteins tested. Additionally, clues about individual proteins’ functions were obtained from their interactions with each of a panel of ligands.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics
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Bacterial Proteins / isolation & purification
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Chromatography, Affinity / methods*
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Crystallography, X-Ray / methods*
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Electrophoresis, Polyacrylamide Gel
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Escherichia coli / chemistry
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Escherichia coli / genetics
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Ligands
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Mycobacterium tuberculosis / chemistry
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Mycobacterium tuberculosis / genetics
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NADP Transhydrogenases / chemistry
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NADP Transhydrogenases / genetics
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Nucleotides / chemistry*
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Nucleotides / genetics
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Protein Interaction Mapping / methods
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / isolation & purification
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Triazines / chemistry*
Substances
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Bacterial Proteins
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Ligands
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Nucleotides
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Recombinant Proteins
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Triazines
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Cibacron Blue F 3GA
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NADP Transhydrogenases