β2-Adrenergic Receptor Solutions for Structural Biology Analyzed with Microscale NMR Diffusion Measurements

Authors

  • Dr. Reto Horst,

    Corresponding author
    1. Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037 (USA)
    • Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037 (USA)

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    • These authors contributed equally to the work.

  • Dr. Pawel Stanczak,

    1. Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037 (USA)
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    • These authors contributed equally to the work.

  • Prof. Dr. Raymond C. Stevens,

    1. Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037 (USA)
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  • Prof. Dr. Kurt Wüthrich

    Corresponding author
    1. Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037 (USA)
    2. Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037 (USA)
    • Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037 (USA)

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  • This work was supported by the NIH Roadmap initiative grant P50 GM073197 for technology development and the PSI:Biology grant U54 GM094618. for GPCR biology studies. The authors thank Jeffrey J. Liu for a critical reading of the manuscript.

Abstract

original image

Microcoil NMR measurements were performed to determine the final composition of solutions of the β2-adrenergic receptor (β2AR) reconstituted with a detergent and to study the hydrodynamic properties of the detergent micelles containing β2AR (see picture). Standards are established for the reproducible preparation of G-protein-coupled receptor solutions for crystallization trials and solution NMR studies.

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