111kHz CPMAS 0.7mm Probe

During the last couple of years magic angle spinning at very high spinning rates (> 100 kHz) opened new opportunities and new application fields in solid state NMR. Having shown investigations of structure and dynamics of large and biologically important proteins like the membrane protein AlkL or the enzyme human carbonic anhydrase II. The feasibility to investigate large, non-deuterated, molecules with proton-detected solid-state NMR, opens-up new opportunities for determination of structure and dynamics for biological samples. By using the 0.7mm CPMAS Probe now, Cryo-EM or high-resolution NMR studies can be efficiently supplemented helping to reveal more details in challenging samples.

But not only applications in biological systems are evolving under very fast magic angle spinning, also studies of systems with highly anisotropic features (e.g., paramagnetic environments) can benefit dramatically if studied using very fast MAS rates.
 

• Very Fast MAS up to 111kHz
  
• Strong and reliable RF performance
  
• MAS stability better than 0.25 % at 111kHz MAS (±28 Hz_max)
• Sample insert and eject without removing the probe from magnet
  
• Available in multiple RF configurations
  - HX
  - HXY
  - HCN
  - HCND
• For all field strengths and SB+WB magnets
   

Electronics: MAS3 unit is required for controlling a 0.7mm CPMAS probe. The probe is not compatible with MAS1 or MAS2 units

Magnets: all SB/WB if probe length matches shim-stack length

Software: ≥TS 3.5 for full functionality of MAS 3 unit. If operated via webpage in standalone mode also older versions are supported
 

Highly resolved spectra from fully protonated biological samples

In addition to the cross-polarization transfer (CP) for multidimensional NMR, polarization can be transferred via INEPT, as known from high resolution NMR.

High sensitivity due to proton detection enables investigation of large samples at natural abundance.

¹H ¹H distances up to a range of 9 Å, comparable to liquid state 1H NOESY can be measured. Combined with the absence of a general limitation of molecular size in solid state NMR, the additional availability of sidechain protons opens new horizons for structural investigations.
 

A β-barrel for oil transport through lipid membranes: Dynamic NMR structures of AlkL
Tobias Schubeis, Tanguy Le Marchand, Csaba Daday, Wojciech Kopec, Kumar Tekwani Movellan, Jan Stanek, Tom S. Schwarzer, Kathrin Castiglione, Bert L. de Groot, Guido Pintacuda, and Loren B. Andreas, PNAS, 2020.
https://doi.org/10.1073/pnas.2002598117

Assessment of a Large Enzyme–Drug Complex by Proton‐Detected Solid‐State NMR Spectroscopy without Deuteration
Suresh K. Vasa, Himanshu Singh, Kristof Grohe and Rasmus Linser, Angew. Chem. Int. Ed. 2019, 58, 5758.
https://doi.org/10.1002/anie.201811714

Structural Analysis of an Antigen Chemically-Coupled on Virus-Like Particles in Vaccine Formulation
K. Jaudzems, A. Kirsteina T. Schubeis G. Casano, O. Ouari. J. Bogans, A. Kazaks, K. Tars, A. Lesage, G. Pintacuda, Angew. Chem. Int. Ed., 2021.
DOI: 10.1002/anie.202013189

Insight into small molecule binding to the neonatal Fc receptor by X-ray crystallography and 100 kHz magic-angle-spinning NMR
Daniel Stöppler, Alex Macpherson, Susanne Smith-Penzel, Nicolas Basse, Fabien Lecomte, Hervé Deboves, Richard D. Taylor, Tim Norman, John Porter, Lorna C. Waters, Marta Westwood, Ben Cossins, Katharine Cain, James White, Robert Griffin, Christine Prosser, Sebastian Kelm, Amy H. Sullivan, David Fox III, Mark D. Carr, Alistair Henry, Richard Taylor, Beat H. Meier, Hartmut Oschkinat, Alastair D. Lawson, Plos Biology, 2018.
https://doi.org/10.1371/journal.pbio.2006192

Picometer Resolution Structure of the Coordination Sphere in the Metal-Binding Site in a Metalloprotein by NMR
Andrea Bertarello, Ladislav Benda, Kevin J. Sanders, Andrew J. Pell, Michael J. Knight, Vladimir Pelmenschikov, Leonardo Gonnelli, Isabella C. Felli, Martin Kaupp, Lyndon Emsley, Roberta Pierattelli and Guido Pintacuda, J. Am. Chem. Soc. 2020, 142, 39, 16757–16765.
DOI: 10.1021/jacs.0c07339

Magic-Angle Spinning Frequencies beyond 300 kHz Are Necessary to Yield Maximum Sensitivity in Selectively Methyl Protonated Protein Samples in Solid-State NMR
Kai Xue, Riddhiman Sarkar, Carina Motz, Sam Asami, Venita Decker, Sebastian Wegner, Zdenek Tosner, and Bernd Reif, J. Phys. Chem. C, 2018, 122, 28, 16437–16442.
DOI: 10.1021/acs.jpcc.8b05600

Selective ¹H–¹H Distance Restraints in Fully Protonated Proteins by Very Fast Magic-Angle Spinning Solid-State NMR
Mukul G. Jain, Daniela Lalli, Jan Stanek, Chandrakala Gowda†, Satya Prakash, Tom S. Schwarzer, Tobias Schubeis, Kathrin Castiglione, Loren B. Andreas, P. K. Madhu, Guido Pintacuda, and Vipin Agarwal, J. Phys. Chem. Lett. 2017, 8, 11, 2399–2405
DOI: 10.1021/acs.jpclett.7b00983

Structure of fully protonated proteins by proton-detected magic-angle spinning NMR
Loren B. Andreas, Kristaps Jaudzems, Jan Stanek, Daniela Lalli, Andrea Bertarello, Tanguy Le Marchand, Diane Cala-De Paepe, Svetlana Kotelovica, Inara Akopjana, Benno Knott, Sebastian Wegner, Frank Engelke, Anne Lesage, Lyndon Emsley, Kaspars Tars, Torsten Herrmann and Guido Pintacuda, PNAS, 2016, 113 (33), 9187-9192.
DOI: 10.1073/pnas.1602248113
 

Quantification of frictional heating at ultra-fast magic-angle spinning.

This application note provides information about how much a sample is heated by air friction when it is spun up until 111 kHz. Further it is described how to determine the sample heating for individual 0.7mm probes.

Tempspin: A new TopSpin tool to automatically compensate frictional heating.

The application notes provide a description and a manual for the new topspin tool tempspin. The tool assists by controlling the sample-temperature while magic-angle-spinning via VT and is usable for all Bruker MAS probes. The tool is part of the new TopSpin release and can be called via TopSpin command line by typing “tempspin”.

Exact Internuclear Distance Determination using the New Tool of the Dynamics Center “Exact Solid-State Distances”

The tool “exact SolidState distances” of the Bruker Dynamics Center leads to reliable internuclear distance restraints in a fast and easy manner. The exported distance restraints can be directly used for structure determination by the program CYNA, ARIA and CNS or MD simulations restrained by NMR data. The results are precise protein structures and directional-dynamics information, which are valuable for structural biology.