Get access

Studies on the MxiH Protein in T3SS Needles Using DNP-Enhanced ssNMR Spectroscopy

Authors

  • Pascal Fricke,

    1. Max Planck Institute for Biophysical Chemistry, Dept. of NMR-based Structural Biology, Am Faßberg 11, 37077 Göttingen (Germany)
    Search for more papers by this author
  • Jean-Philippe Demers,

    1. Max Planck Institute for Biophysical Chemistry, Dept. of NMR-based Structural Biology, Am Faßberg 11, 37077 Göttingen (Germany)
    Search for more papers by this author
  • Dr. Stefan Becker,

    1. Max Planck Institute for Biophysical Chemistry, Dept. of NMR-based Structural Biology, Am Faßberg 11, 37077 Göttingen (Germany)
    Search for more papers by this author
  • Dr. Adam Lange

    Corresponding author
    1. Max Planck Institute for Biophysical Chemistry, Dept. of NMR-based Structural Biology, Am Faßberg 11, 37077 Göttingen (Germany)
    • Max Planck Institute for Biophysical Chemistry, Dept. of NMR-based Structural Biology, Am Faßberg 11, 37077 Göttingen (Germany)

    Search for more papers by this author

Abstract

Bacterial T3SS needles formed by the protein MxiH are studied using DNP-enhanced ssNMR spectroscopy at 14.1 T (600 MHz). This technique provides spectra of good resolution, allowing us to draw conclusions about the protein dynamics. With the obtained signal enhancement, samples of limited quantity now get within reach of ssNMR studies.

Ancillary