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. With the advent of faster magic-angle spinning (MAS) andhigher magnetic fields, the resolution of biomolecular solid-state nuclearmagnetic resonance (NMR) spectra has been continuously increasing. As adirect consequence, the always narrower spectral lines, especially inproton-detected spectroscopy, are also becoming more sensitive to temporalinstabilities of the magnetic field in the sample volume. Field drifts inthe order of tenths of parts per million occur after probe insertion or temperaturechange, during cryogen refill, or are intrinsic to the superconductinghigh-field magnets, particularly in the months after charging. As an alternative to a field–frequency lock based on deuterium solventresonance rarely available for solid-state NMR, we present a strategy tocompensate non-linear field drifts using simultaneous acquisition of afrequency reference (SAFR). It is based on the acquisition of an auxiliary1D spectrum in each scan of the experiment. Typically, a small-flip-anglepulse is added at the beginning of the pulse sequence. Based on thefrequency of the maximum of the solvent signal, the field evolution in timeis reconstructed and used to correct the raw data after acquisition, therebyacting in its principle as a digital lock system. The general applicabilityof our approach is demonstrated on 2D and 3D protein spectra during varioussituations with a non-linear field drift. SAFR with small-flip-angle pulsescauses no significant loss in sensitivity or increase in experimental timein protein spectroscopy. The correction leads to the possibility ofrecording high-quality spectra in a typical biomolecular experiment evenduring non-linear field changes in the order of 0.1 ppm h−1 without theneed for hardware solutions, such as stabilizing the temperature of themagnet bore. The improvement of linewidths and peak shapes turns out to beespecially important for 1H-detected spectra under fast MAS, but themethod is suitable for the detection of carbon or other nuclei as well.

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