Articles | Volume 1, issue 2
https://doi.org/10.5194/mr-1-331-2020
© Author(s) 2020. This work is distributed under
the Creative Commons Attribution 4.0 License.
the Creative Commons Attribution 4.0 License.
https://doi.org/10.5194/mr-1-331-2020
© Author(s) 2020. This work is distributed under
the Creative Commons Attribution 4.0 License.
the Creative Commons Attribution 4.0 License.
Research article
| 
23 Dec 2020
Research article |
| 23 Dec 2020
| 23 Dec 2020
ssNMRlib: a comprehensive library and tool box for acquisition of solid-state nuclear magnetic resonance experiments on Bruker spectrometers
Alicia Vallet
CORRESPONDING AUTHOR
Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS), 71, Avenue des Martyrs, 38044 Grenoble, France
Adrien Favier
Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS), 71, Avenue des Martyrs, 38044 Grenoble, France
Bernhard Brutscher
Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS), 71, Avenue des Martyrs, 38044 Grenoble, France
Univ. Grenoble Alpes, CEA, CNRS, Institut de Biologie Structurale (IBS), 71, Avenue des Martyrs, 38044 Grenoble, France
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- Deuteration of proteins boosted by cell lysates: high-resolution amide and Hα magic-angle-spinning (MAS) NMR without the reprotonation bottleneck F. Napoli et al. https://doi.org/10.5194/mr-5-33-2024
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- OPTO: Automated Optimization for Solid-State NMR Spectroscopy C. Borcik et al. https://doi.org/10.1021/jacs.4c13295
- Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD D. Gauto et al. https://doi.org/10.1016/j.yjsbx.2022.100079
- Protein resonance assignment by solid-state NMR based on 1H-detected 13C double-quantum spectroscopy at fast MAS A. Lends et al. https://doi.org/10.1007/s10858-021-00386-6
- Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR D. Gauto et al. https://doi.org/10.1038/s41467-022-29423-0
- Disulfide-Bond-Induced Structural Frustration and Dynamic Disorder in a Peroxiredoxin from MAS NMR L. Troussicot et al. https://doi.org/10.1021/jacs.3c01200
- Staphylococcus aureus sacculus mediates activities of M23 hydrolases A. Razew et al. https://doi.org/10.1038/s41467-023-42506-w
- The hepatitis E virus capsid protein forms amyloid-like fibrils that sequester TANK-binding kinase 1 to dampen antiviral responses P. Jordan et al. https://doi.org/10.1016/j.celrep.2026.117513
- Automation in solid state NMR C. Johann et al. https://doi.org/10.1016/j.jmr.2023.107554
- Aromatic ring flips reveal reshaping of protein dynamics in crystals and complexes L. Becker et al. https://doi.org/10.1038/s41557-026-02155-0
- 1H-Detected Biomolecular NMR under Fast Magic-Angle Spinning T. Le Marchand et al. https://doi.org/10.1021/acs.chemrev.1c00918
- Bumps on the Road: The Way to Clean Relaxation Dispersion Magic-Angle Spinning NMR B. Tatman et al. https://doi.org/10.1021/jacs.5c09057
- Structural characterization, DFT studies, and therapeutic potential of selenium Schiff base-derived transition metal complexes (Co(II), Ni(II), Cu(II), and Zn(II) A. Ali et al. https://doi.org/10.1016/j.molstruc.2026.147574
- Accelerating 15N and 13C R1 and R1ρ relaxation measurements by multiple pathway solid-state NMR experiments J. Tognetti et al. https://doi.org/10.1016/j.jmr.2021.107049
- A modular library for fast prototyping of solution-state nuclear magnetic resonance experiments M. Górka & W. Koźmiński https://doi.org/10.5194/mr-5-51-2024
Saved (final revised paper)
Latest update: 14 Oct 2026
Short summary
We introduce ssNMRlib, a library of pulse sequences and jython scripts for user-friendly setup and acquisition of solids-state NMR experiments. ssNMRlib facilitates all steps of data acquisition, including calibration of various pulse-sequence parameters and semi-automatic setup of even complex high-dimensional experiments, using an intuitive graphical user interface, launched directly within Bruker's Topspin acquisition program.
We introduce ssNMRlib, a library of pulse sequences and jython scripts for user-friendly setup...
