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Default Integrated analysis of the conformation of a protein-linked spin label by crystallography, EPR and NMR spectroscopy

Integrated analysis of the conformation of a protein-linked spin label by crystallography, EPR and NMR spectroscopy


Abstract Long-range structural information derived from paramagnetic relaxation enhancement observed in the presence of a paramagnetic nitroxide radical is highly useful for structural characterization of globular, modular and intrinsically disordered proteins, as well as proteinÔ??protein and protein-DNA complexes. Here we characterized the conformation of a spin-label attached to the homodimeric protein CylR2 using a combination of X-ray crystallography, electron paramagnetic resonance (EPR) and NMR spectroscopy. Close agreement was found between the conformation of the spin label observed in the crystal structure with interspin distances measured by EPR and signal broadening in NMR spectra, suggesting that the conformation seen in the crystal structure is also preferred in solution. In contrast, conformations of the spin label observed in crystal structures of T4 lysozyme are not in agreement with the paramagnetic relaxation enhancement observed for spin-labeled CylR2 in solution. Our data demonstrate that accurate positioning of the paramagnetic center is essential for high-resolution structure determination.
  • Content Type Journal Article
  • Pages 1-9
  • DOI 10.1007/s10858-011-9471-y
  • Authors
    • Tim Gruene, Department of Structural Chemistry, University of G├Âttingen, Tammannstra├?e 4, 37077 G├Âttingen, Germany
    • Min-Kyu Cho, Department of NMR based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fa├?berg 11, 37077 G├Âttingen, Germany
    • Irina Karyagina, Max Planck Institute for Biophysical Chemistry, AG Electron Spin Resonance Spectroscopy, Am Fa├?berg 11, 37077 G├Âttingen, Germany
    • Hai-Young Kim, Department of NMR based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fa├?berg 11, 37077 G├Âttingen, Germany
    • Christian Grosse, Department of Structural Chemistry, University of G├Âttingen, Tammannstra├?e 4, 37077 G├Âttingen, Germany
    • Karin Giller, Department of NMR based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fa├?berg 11, 37077 G├Âttingen, Germany
    • Markus Zweckstetter, Department of NMR based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fa├?berg 11, 37077 G├Âttingen, Germany
    • Stefan Becker, Department of NMR based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fa├?berg 11, 37077 G├Âttingen, Germany

Source: Journal of Biomolecular NMR
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