Articles | Volume 3, issue 1
Research article
09 Feb 2022
Research article |  | 09 Feb 2022

Correction of field instabilities in biomolecular solid-state NMR by simultaneous acquisition of a frequency reference

Václav Římal, Morgane Callon, Alexander A. Malär, Riccardo Cadalbert, Anahit Torosyan, Thomas Wiegand, Matthias Ernst, Anja Böckmann, and Beat H. Meier

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Cited articles

Böckmann, A., Gardiennet, C., Verel, R., Hunkeler, A., Loquet, A., Pintacuda, G., Emsley, L., Meier, B. H., and Lesage, A.: Characterization of different water pools in solid-state NMR protein samples, J. Biomol. NMR, 45, 319–327,, 2009. 
Bodenhausen, G., Kogler, H., and Ernst, R. R.: Selection of coherence-transfer pathways in NMR pulse experiments, J. Magn. Reson., 58, 370–388,, 1984. 
Gallo, A., Franks, W. T., and Lewandowski, J. R.: A suite of solid-state NMR experiments to utilize orphaned magnetization for assignment of proteins using parallel high and low gamma detection, J. Magn. Reson., 305, 219–231,, 2019. 
Gopinath, T. and Veglia, G.: Proton-detected polarization optimized experiments (POE) using ultrafast magic angle spinning solid-state NMR: Multi-acquisition of membrane protein spectra, J. Magn. Reson., 310, 106664,, 2020. 
Short summary
Through the advent of fast magic-angle spinning and high magnetic fields, the spectral resolution of solid-state NMR spectra has recently been greatly improved. To take full advantage of this gain, the magnetic field must be stable over the experiment time of hours or even days. We thus monitor the field by simultaneous acquisition of a frequency reference (SAFR) and use this information to correct multidimensional spectra improving resolution and availability of productive magnet time.