Over the past few decades, advances in NMR of biological solids have been largely driven by the development of magic angle spinning (MAS) probes at increasingly higher frequencies. The introduction of ultrafast MAS technologies, which significantly reduce linewidths, has opened the way to a wide range of applications of solid-state NMR, particularly for the study of complex proteins such as integral membrane proteins, prions, and viral capsids.

In a recent communication, researchers from the Infranalytics site in Lyon present the first results obtained with a new-generation MAS probe, capable of rotating the sample at 160 kHz. These data reveal a significant improvement in spectral resolution, both for a microcrystallized protein and for a membrane protein reconstituted in a lipid bilayer. This advance is made possible by the optimization of sample handling, rotor filling, and experimental conditions, thus opening new perspectives for structural biology.

Link to the article: https://pubs.acs.org/doi/abs/10.1021/jacs.5c02466