Structural Analysis of Large Protein Complexes Using Solvent Paramagnetic Relaxation Enhancements

Authors

  • Dr. Tobias Madl,

    1. Institute of Structural Biology, Helmholtz Zentrum München, Biomolecular NMR and Center for Integrated Protein Science Munich, Department Chemie, Technische Universität München, Lichtenbergstrasse 4, 85747 Garching (Germany), Fax: (+49) 89-289-13867 http://www.helmholtz-muenchen.de/stb
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  • Dr. Thomas Güttler,

    1. Max-Planck-Institut für biophysikalische Chemie, Am Fassberg 11, 37077 Göttingen (Germany)
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  • Prof. Dr. Dirk Görlich,

    1. Max-Planck-Institut für biophysikalische Chemie, Am Fassberg 11, 37077 Göttingen (Germany)
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  • Prof. Dr. Michael Sattler

    Corresponding author
    1. Institute of Structural Biology, Helmholtz Zentrum München, Biomolecular NMR and Center for Integrated Protein Science Munich, Department Chemie, Technische Universität München, Lichtenbergstrasse 4, 85747 Garching (Germany), Fax: (+49) 89-289-13867 http://www.helmholtz-muenchen.de/stb
    • Institute of Structural Biology, Helmholtz Zentrum München, Biomolecular NMR and Center for Integrated Protein Science Munich, Department Chemie, Technische Universität München, Lichtenbergstrasse 4, 85747 Garching (Germany), Fax: (+49) 89-289-13867 http://www.helmholtz-muenchen.de/stb===

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  • We thank the Bavarian NMR Center (BNMRZ) for NMR measurement time. This study was supported by the EMBO (fellowship to T.M.), the Austrian Science Fund (FWF, Schrödinger fellowship to T.M.), the Max-Planck-Gesellschaft, the Boehringer Ingelheim Fonds, the Alfried Krupp von Bohlen und Halbach Foundation (fellowships to T.G.), and the European Commission contracts 3D Repertoire (LSHG-CT-2005-512028), NIM3 (No. 226507), and EU-NMR (No. RII3-026145).

Abstract

original image

The solvent helps out: Conventional protocols for structural analysis of protein complexes often fail if only sparse experimental data are available. NMR-spectroscopy-derived solvent paramagnetic relaxation enhancements (PREs) from a soluble spin label (picture) significantly improve the structural quality of a 150 kDa protein complex. This general protocol is an efficient approach for structural analysis of large protein complexes in solution.

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