Crystal structure of the Escherichia coli Tas protein, an NADP(H)-dependent aldo-keto reductase

Authors

  • Galina Obmolova,

    1. Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute and the National Institute of Standards and Technology, Rockville, Maryland
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  • Alexey Teplyakov,

    1. Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute and the National Institute of Standards and Technology, Rockville, Maryland
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  • Pavel P. Khil,

    1. Genetics and Biochemistry Branch, NIDDK, National Institutes of Health, Bethesda, Maryland
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  • Andrew J. Howard,

    1. Center for Synchrotron Radiation Research and Instrumentation, Biological, Chemical and Physical Sciences Department, Illinois Institute of Technology, Chicago, Illinois
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  • R. Daniel Camerini-Otero,

    1. Genetics and Biochemistry Branch, NIDDK, National Institutes of Health, Bethesda, Maryland
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  • Gary L. Gilliland

    Corresponding author
    1. Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute and the National Institute of Standards and Technology, Rockville, Maryland
    • Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, and the National Institute of Standards and Technology, 9600 Gudelsky Drive, Rockville, MD 20850
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  • Certain commercial materials, instruments, and equipment are identified in this article to specify the experimental procedure as completely as possible. In no case does such identification imply a recommendation or endorsement by the National Institute of Standards and Technology nor does it imply that the materials, instruments, or equipment identified is necessarily the best available for the purpose.

    The accepted SI units of concentration, mol/L, and of unified atomic mass unit, u, have been represented by the symbols M and Da, respectively, to conform to the conventions of this journal.

No abstract is available for this article.

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