Protein structure determination from 13C spin-diffusion solid-state NMR spectroscopy.
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.
Manolikas
Theofanis
T
Physical Chemistry, ETH Zurich, CH-8093 Zurich, Switzerland.
Herrmann
Torsten
T
Meier
Beat H
BH
D002247:Carbon Isotopes; D018360:Crystallography, X-Ray; D004058:Diffusion; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D025801:Ubiquitin / Q000737:chemistry*
D002247:Carbon Isotopes; D025801:Ubiquitin