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About Solution NMR, Grenoble, France

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Solution NMR

Researchers can gain access to 950, 850, 700, and several 600 MHz instruments, equipped with most recent Bruker electronics (Avance III HD) and cryogenically cooled probes for high-sensitivity solution-state NMR applications. Standard Bruker experiment libraries, as well as additional in-house libraries for optimised fast NMR data acquisition (e.g. SOFAST, BEST, and HADAMAC-type experiments) are available. Fast-mixing equipments required for real-time studies of kinetic processes such as protein folding are also available.

Instruments Available:

Special accesory: Automatic sample changer for up to 24 NMR tubes Liquid-state probes: Cryo TCI (1H, 13C, 15N, 2H), 5 mm, z-gradients, Cryo TCI (1H, 13C, 15N, 2H), 1.7 mm, z-gradients

950 MHz Bruker Avance IIIHD (22.3 T) Special accessory: Automatic sample changer for up to 24 NMR tubes Liquid-state probes: Cryo TCI (1H, 13C, 15N, 2H), 5 mm, z-gradients (0° Solid-state probes: MAS (1H, 13C, 15N), 3.2 mm, E-free (νr< 25 kHz) - MAS (1H, 13C, 15N), 1.3 mm, +lock(νr< 60 kHz)

User Guide

For more information, please visit the IBS NMR facility website.

 

For iNEXT-Discovery applications

Scientific background, significance and objectives

Please describe the general scientific background for your project, explain - to a non-expert in the biology of the system - why these questions are important, and clearly at the end define your objectives, in terms of the tangible results you want to obtain and the questions these results will help to address.

Project background in your lab & recent results

Please describe if preliminary 1D 1H NMR spectra or 2D 1H-15N-HSQC spectra have been already acquired on your target samples. Describe if you have already performed a screen for conditions, such as buffer optimization, that promote stability (with respect to slow precipitation) or better quality NMR spectra. Please provide the NMR sample molecular weight and the concentration that you are able to reach without precipitation. Possibly, a priori knowledge of the oligomerization state of the system is critical to sample labeling choice. Please provide preliminary information about oligomerization state of your system, if you have it.

Research required, requested

Please describe what are the exact questions that you need to answer. This will allow us to determine a list of the NMR experiments needed in order to characterize your system. To get structural information on proteins by solution NMR, isotopically labelled samples, usually 15N and/or 15N/13C, are required. For proteins with MW > 20 kDa, protein 2H labelling (partial or complete depending on the MW) is also needed. If you are unsure of the optimal method to address your question, please state this openly and use this space to explain as well as possible what are the exact questions that you need to answer; this will not affect your proposal negatively as part of our mission is to suggest the best experiment(s) for answering user questions.

Benefit for health, food, biotechnology or biomaterials

Please include a statement for the immediate or longer-term impact that your research might have in innovations related to the fields above. These do not need to lead to a “product” but to scientific or technical innovations that can be of value for translational research in any of the sectors above.

Instruct Centre

Instruct Centre FR2

IBS-ISBG

71 avenue des Martyrs

Grenoble

France

www.ibs.fr & www.isbg.fr

Solution NMR, Grenoble, France

Contacts:

Adrien Favier
Adrien Favier
Institut de Biologie Structurale
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Bernhard Brutscher
Bernhard Brutscher
Institut de Biologie Structurale
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