Gor'kov, P. L., Witter, R., Chekmenev, E. Y., Nozirov, F., Fu, R., and Brey,
W. W.: Low-E probe for
19F–
1H NMR of dilute biological solids, J.
Magn. Reson., 189, 182–189, https://doi.org/10.1016/j.jmr.2007.09.008,
2007.
Gottlieb, H. E., Kotlyar, V., and Nudelman, A.: NMR Chemical Shifts of Common
Laboratory Solvents as Trace Impurities, J. Org. Chem., 62, 7512–7515,
https://doi.org/10.1021/jo971176v, 1997.
Henry, P.-G., van de Moortele, P.-F., Giacomini, E., Nauerth, A., and Bloch,
G.: Field-frequency locked in vivo proton MRS on a whole-body spectrometer,
Magn. Reson. Med., 42, 636–642,
https://doi.org/10.1002/(SICI)1522-2594(199910)42:4<636::AID-MRM4>3.0.CO;2-I, 1999.
Kupče, Ē. and Claridge, T. D. W.: NOAH: NMR Supersequences for Small
Molecule Analysis and Structure Elucidation, Angew. Chem. Int. Ed., 56,
11779–11783, https://doi.org/10.1002/anie.201705506, 2017.
Kupče, Ē. and Freeman, R.: Molecular structure from a single NMR
sequence (fast-PANACEA), J. Magn. Reson., 206, 147–153,
https://doi.org/10.1016/j.jmr.2010.06.018, 2010.
Lacabanne, D., Fogeron, M.-L., Wiegand, T., Cadalbert, R., Meier, B. H., and
Böckmann, A.: Protein sample preparation for solid-state NMR
investigations, Prog. Nucl. Mag. Res. Sp., 110, 20–33,
https://doi.org/10.1016/j.pnmrs.2019.01.001, 2019.
Malär, A. A., Völker, L. A., Cadalbert, R., Lecoq, L., Ernst, M.,
Böckmann, A., Meier, B. H., and Wiegand, T.: Temperature-Dependent
Solid-State NMR Proton Chemical-Shift Values and Hydrogen Bonding, J. Phys.
Chem. B, 125, 6222–6230, https://doi.org/10.1021/acs.jpcb.1c04061,
2021.
Minkler, M. J., Kim, J. M., Shinde, V. V., and Beckingham, B. S.: Low-field
1H NMR spectroscopy: Factors impacting signal-to-noise ratio and
experimental time in the context of mixed microstructure polyisoprenes,
Magn. Reson. Chem., 58, 1168–1176, https://doi.org/10.1002/mrc.5022,
2020.
Najbauer, E. E. and Andreas, L. B.: Correcting for magnetic field drift in
magic-angle spinning NMR datasets, J. Magn. Reson., 305, 1–4,
https://doi.org/10.1016/j.jmr.2019.05.005, 2019.
Near, J., Edden, R., Evans, C. J., Paquin, R., Harris, A., and Jezzard, P.:
Frequency and phase drift correction of magnetic resonance spectroscopy data
by spectral registration in the time domain, Magn. Reson. Med., 73,
44–50, https://doi.org/10.1002/mrm.25094, 2015.
Nimerovsky, E., Movellan, K. T., Zhang, X. C., Forster, M. C., Najbauer, E.,
Xue, K., Dervişoglu, R., Giller, K., Griesinger, C., Becker, S., and
Andreas, L. B.: Proton Detected Solid-State NMR of Membrane Proteins at 28 Tesla (1.2 GHz) and 100 kHz Magic-Angle Spinning, Biomolecules, 11, 752,
https://doi.org/10.3390/biom11050752, 2021.
Paulson, E. K. and Zilm, K. W.: External field-frequency lock probe for high
resolution solid state NMR, Rev. Sci. Instrum., 76, 026104,
https://doi.org/10.1063/1.1841972, 2005.
Penzel, S., Oss, A., Org, M. L., Samoson, A., Böckmann, A., Ernst, M.
and Meier, B. H.: Spinning faster: protein NMR at MAS frequencies up to
126 kHz, J. Biomol. NMR, 73, 19–29,
https://doi.org/10.1007/s10858-018-0219-9, 2019.
Press, W. H., Teukolsky, S. A., Vetterling, W. T., and Flannery, B. P.:
Minimization or Maximization of Functions, in: Numerical Recipes in C: The
Art of Scientific Computing, 2nd edn., 394–455, Cambridge University Press,
Cambridge, ISBN 0-521-43108-5, 1992.
Ravotti, F., Sborgi, L., Cadalbert, R., Huber, M., Mazur, A., Broz, P.,
Hiller, S., Meier, B. H., and Böckmann, A.: Sequence-specific solid-state
NMR assignments of the mouse ASC PYRIN domain in its filament form, Biomol.
NMR Assign., 10, 107–115, https://doi.org/10.1007/s12104-015-9647-6,
2016.
Římal, V.: Pulse and AU programs for correcting field instabilities
in NMR by simultaneous acquisition of a frequency reference (SAFR), ETH
Zurich [code], https://doi.org/10.5905/ethz-1007-485, 2022.
Římal, V., Callon, M., Malär, A. A., Cadalbert, R., Torosyan, A., Wiegand, T., Ernst, M., Böckmann, A., and Meier, B. H.:
Experimental Data for Correction of
Field Instabilities in Biomolecular Solid-State NMR by Simultaneous
Acquisition of a Frequency Reference, ETH Zurich [data set],
https://doi.org/10.3929/ethz-b-000522147, 2021.
Sborgi, L., Ravotti, F., Dandey, V. P., Dick, M. S., Mazur, A., Reckel, S.,
Chami, M., Scherer, S., Huber, M., Böckmann, A., Egelman, E. H.,
Stahlberg, H., Broz, P., Meier, B. H., and Hiller, S.: Structure and assembly
of the mouse ASC inflammasome by combined NMR spectroscopy and cryo-electron
microscopy, P. Natl. Acad. Sci., 112, 13237–13242,
https://doi.org/10.1073/pnas.1507579112, 2015.
Sharma, K., Madhu, P. K., and Mote, K. R.: A suite of pulse sequences based
on multiple sequential acquisitions at one and two radiofrequency channels
for solid-state magic-angle spinning NMR studies of proteins, J. Biomol.
NMR, 65, 127–141, https://doi.org/10.1007/s10858-016-0043-z, 2016.
Stanek, J., Schubeis, T., Paluch, P., Güntert, P., Andreas, L. B., and
Pintacuda, G.: Automated Backbone NMR Resonance Assignment of Large Proteins
Using Redundant Linking from a Single Simultaneous Acquisition, J. Am. Chem.
Soc., 142, 5793–5799, https://doi.org/10.1021/jacs.0c00251, 2020.
States, D., Haberkorn, R., and Ruben, D.: A two-dimensional nuclear
Overhauser experiment with pure absorption phase in four quadrants, J. Magn.
Reson., 48, 286–292, https://doi.org/10.1016/0022-2364(82)90279-7, 1982.
Stevens, T. J., Fogh, R. H., Boucher, W., Higman, V. A., Eisenmenger, F.,
Bardiaux, B., Van Rossum, B. J., Oschkinat, H., and Laue, E. D.: A software
framework for analysing solid-state MAS NMR data, J. Biomol. NMR, 51,
437–447, https://doi.org/10.1007/s10858-011-9569-2, 2011.
Takegoshi, K., Nakamura, S., and Terao, T.:
13C–
1H dipolar-assisted
rotational resonance in magic-angle spinning NMR, Chem. Phys. Lett.,
344, 631–637, https://doi.org/10.1016/S0009-2614(01)00791-6, 2001.
Takegoshi, K., Nakamura, S., and Terao, T.:
13C–
1H dipolar-driven
13C–
13C recoupling without
13C rf irradiation in nuclear
magnetic resonance of rotating solids, J. Chem. Phys., 118, 2325–2341,
https://doi.org/10.1063/1.1534105, 2003.
Takahashi, M., Ebisawa, Y., Tennmei, K., Yanagisawa, Y., Hosono, M.,
Takasugi, K., Hase, T., Miyazaki, T., Fujito, T., Nakagome, H., Kiyoshi, T.,
Yamazaki, T., and Maeda, H.: Towards a beyond 1 GHz solid-state nuclear
magnetic resonance: External lock operation in an external current mode for
a 500 MHz nuclear magnetic resonance, Rev. Sci. Instrum., 83, 105110,
https://doi.org/10.1063/1.4757576, 2012.
Thiel, T., Czisch, M., Elbel, G. K., and Hennig, J.: Phase coherent averaging
in magnetic resonance spectroscopy using interleaved navigator scans:
Compensation of motion artifacts and magnetic field instabilities, Magn.
Reson. Med., 47, 1077–1082, https://doi.org/10.1002/mrm.10174, 2002.
Torosyan, A., Wiegand, T., Schledorn, M., Klose, D., Güntert, P.,
Böckmann, A., and Meier, B. H.: Including Protons in Solid-State NMR
Resonance Assignment and Secondary Structure Analysis: The Example of RNA
Polymerase II Subunits Rpo
, Front. Mol. Biosci., 6, 100,
https://doi.org/10.3389/fmolb.2019.00100, 2019.
Van Melckebeke, H., Wasmer, C., Lange, A., AB, E., Loquet, A.,
Böckmann, A., and Meier, B. H.: Atomic-Resolution
Three-Dimensional Structure of HET-s(218
−289) Amyloid Fibrils by
Solid-State NMR Spectroscopy, J. Am. Chem. Soc., 132, 13765–13775,
https://doi.org/10.1021/ja104213j, 2010.
Verel, R., Ernst, M., and Meier, B. H.: Adiabatic dipolar recoupling in
solid-state NMR: The DREAM scheme, J. Magn. Reson., 150, 81–99,
https://doi.org/10.1006/jmre.2001.2310, 2001.
Vionnet, L., Aranovitch, A., Duerst, Y., Haeberlin, M., Dietrich, B. E.,
Gross, S., and Pruessmann, K. P.: Simultaneous feedback control for joint
field and motion correction in brain MRI, Neuroimage, 226, 117286,
https://doi.org/10.1016/j.neuroimage.2020.117286, 2021.
Vranken, W. F., Boucher, W., Stevens, T. J., Fogh, R. H., Pajon, A., Llinas,
M., Ulrich, E. L., Markley, J. L., Ionides, J., and Laue, E. D.: The CCPN
data model for NMR spectroscopy: Development of a software pipeline,
Proteins, 59, 687–696,
https://doi.org/10.1002/prot.20449, 2005.
Werner, F. and Grohmann, D.: Evolution of multisubunit RNA polymerases in
the three domains of life, Nat. Rev. Microbiol., 9, 85–98,
https://doi.org/10.1038/nrmicro2507, 2011.
Zhou, D. H. and Rienstra, C. M.: High-performance solvent suppression for
proton detected solid-state NMR, J. Magn. Reson., 192, 167–172,
https://doi.org/10.1016/j.jmr.2008.01.012, 2008.