Transient sedimentation of proteins inside a solid-state NMR rotor under fast magic-angle spinning offers a promising solution to the challenge of determining the structures of high-molecular-weight proteins with atomic resolution. This opens new opportunities for structural analysis of large macromolecules and macromolecular assemblies.
References
Wüthrich, K. Angew. Chem. Int. Ed. 42, 3340–3363 (2002).
Andrew, E. R., Bradbury, A. & Eades, R. G. Nature 182, 1659 (1958).
Lowe, I. J. Phys. Rev. Lett. 2, 285–287 (1959).
Schaefer, J. & Stejskal, E. O. J. Am. Chem. Soc. 98, 1031–1032 (1976).
Bertini, I. et al. Proc. Natl Acad. Sci. USA 108, 10396–10399 (2011).
Mainz, A., Jehle, S., van Rossum, B.-J., Oschkinat, H. & Reif, B. J. Am. Chem. Soc. 131, 15968–15969 (2009).
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Polenova, T. Spinning into focus. Nature Chem 3, 759–760 (2011). https://doi.org/10.1038/nchem.1143
Published:
Issue Date:
DOI: https://doi.org/10.1038/nchem.1143
- Springer Nature Limited
This article is cited by
-
SedNMR: a web tool for optimizing sedimentation of macromolecular solutes for SSNMR
Journal of Biomolecular NMR (2013)
-
On the use of ultracentrifugal devices for sedimented solute NMR
Journal of Biomolecular NMR (2012)