We request funding to acquire a 800 MHz cryoprobe accessory. We have secured funding for a new 800 MHz instrument that will alleviate the long waiting times for and insufficient access to high-field instrumentation. The high-field instruments operating at 750 MHz and above available to the group of investigators asking for this support (Gerhard Wagner, James Chou, Christopher Walsh, Ellis Reinherz and Anders Naar) are limited to one 750 MHz spectrometer and half of a 900 MHz system. Despite this limited access, this group was very successful in determining structures and performing functional studies of very large and challenging systems, such as membrane proteins, complexes of translation initiation factors, non-ribosomal peptide synthetases, transcriptional activator/coactivator complexes, T-cell protein complexes and many more. Numerous new projects are in the pipeline but progress is slowed down due to the lack of access to high field instruments, and waiting times are often two months to get access to the 750 or 900 MHz spectrometers. To alleviate this, we have obtained funds to purchase a non-shielded 800 MHz spectrometer from a Harvard internal competition, and other sources, and we have secured funds to renovate space at the Harvard/MIT Center for Magnetic Resonance to house the new instrument. However, the funds available are only sufficient to purchase the spectrometer with a conventional room temperature probe and are not enough to buy a cryogenic probe. To optimally use the power of this new instrument we ask for funds for a cryoprobe accessory with one cryoplatform and two triple-resonance cryoprobes that are optimized for 1H detection (TCI), which will be the work horse for 3D ad 4D dispersed NOESY experiments, and a 13C/15N detection optimized probe, which will be used for novel experiments that promise to push the limit for studying very large system.

National Institute of Health (NIH)
National Center for Research Resources (NCRR)
Biomedical Research Support Shared Instrumentation Grants (S10)
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Special Emphasis Panel (ZRG1-BCMB-N (30))
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Birken, Steven
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Harvard University
Schools of Medicine
United States
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Viegas, Aldino; Viennet, Thibault; Yu, Tsyr-Yan et al. (2016) UTOPIA NMR: activating unexploited magnetization using interleaved low-gamma detection. J Biomol NMR 64:9-15
Edmonds, Katherine A; Wagner, Gerhard (2015) (1)H, (13)C, and (15)N backbone and sidechain chemical shift assignments for the HEAT2 domain of human eIF4GI. Biomol NMR Assign 9:157-60
Takeuchi, Koh; Sun, Zhen-Yu J; Li, Shuai et al. (2015) NMR resonance assignments of the catalytic domain of human serine/threonine phosphatase calcineurin in unligated and PVIVIT-peptide-bound states. Biomol NMR Assign 9:201-5
Gal, Maayan; Li, Shuai; Luna, Rafael E et al. (2014) The LxVP and PxIxIT NFAT motifs bind jointly to overlapping epitopes on calcineurin's catalytic domain distant to the regulatory domain. Structure 22:1016-27
Elter, Shantha; Raschle, Thomas; Arens, Sabine et al. (2014) The use of amphipols for NMR structural characterization of 7-TM proteins. J Membr Biol 247:957-64
Akabayov, Sabine R; Wagner, Gerhard (2014) Backbone resonance assignment of the HEAT1-domain of the human eukaryotic translation initiation factor 4GI. Biomol NMR Assign 8:89-91
Akabayov, Sabine R; Akabayov, Barak; Richardson, Charles C et al. (2013) Molecular crowding enhanced ATPase activity of the RNA helicase eIF4A correlates with compaction of its quaternary structure and association with eIF4G. J Am Chem Soc 135:10040-7
Etzkorn, Manuel; Raschle, Thomas; Hagn, Franz et al. (2013) Cell-free expressed bacteriorhodopsin in different soluble membrane mimetics: biophysical properties and NMR accessibility. Structure 21:394-401
Hagn, Franz; Etzkorn, Manuel; Raschle, Thomas et al. (2013) Optimized phospholipid bilayer nanodiscs facilitate high-resolution structure determination of membrane proteins. J Am Chem Soc 135:1919-25
Yu, Tsyr-Yan; Raschle, Thomas; Hiller, Sebastian et al. (2012) Solution NMR spectroscopic characterization of human VDAC-2 in detergent micelles and lipid bilayer nanodiscs. Biochim Biophys Acta 1818:1562-9

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