Protein structure determination from 13C spin-diffusion solid-state NMR spectroscopy

J Am Chem Soc. 2008 Mar 26;130(12):3959-66. doi: 10.1021/ja078039s. Epub 2008 Mar 6.


Proton-driven 13C spin diffusion (PDSD) is a simple and robust two-dimensional NMR experiment. It leads to spectra with a high signal-to-noise ratio in which cross-peaks contain information about internuclear distances. We show that the total information content is sufficient to determine the atomic-resolution structure of a small protein from a single, uniformly 13C-, 15N-labeled microcrystalline sample. For the example of ubiquitin, the structure was determined by a manual procedure followed by an automatic optimization of the manual structure as well as by a fully automated structure determination approach. The relationship between internuclear distances and cross-peak intensities in the spectra is investigated.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carbon Isotopes
  • Crystallography, X-Ray
  • Diffusion
  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Protein Conformation
  • Protein Structure, Tertiary
  • Ubiquitin / chemistry*


  • Carbon Isotopes
  • Ubiquitin