Cellular solid-state Nuclear Magnetic Resonance spectroscopy

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Access status: Embargo until 2050-01-01 , 4863.full.pdf (2.87 MB)

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2012

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Renault, M.A.M.ISNI 0000000356699183
Tommassen - van Boxtel, RiaISNI 0000000392955068
Bos, Martine PISNI 0000000388798178
Post, Jan AISNI 0000000387159446
Tommassen, JanISNI 0000000390400608
Baldus, MarcISNI 0000000139673796

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Abstract

Decrypting the structure, function, and molecular interactions of complex molecular machines in their cellular context and at atomic resolution is of prime importance for understanding fundamental physiological processes. Nuclear magnetic resonance is a wellestablished imaging method that can visualize cellular entities at the micrometer scale and can be used to obtain 3D atomic structures under in vitro conditions. Here, we introduce a solid-state NMR approach that provides atomic level insights into cell-associated molecular components. By combining dedicated protein production and labeling schemes with tailored solid-state NMR pulse methods, we obtained structural information of a recombinant integral membrane protein and the major endogenous molecular components in a bacterial environment. Our approach permits studying entire cellular compartments as well as cell-associated proteins at the same time and at atomic resolution.

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Renault, M A M, Tommassen-van Boxtel, H A M, Bos, M P, Post, J A, Tommassen, J P M & Baldus, M 2012, 'Cellular solid-state Nuclear Magnetic Resonance spectroscopy', Proceedings of the National Academy of Sciences of the United States of America, vol. 109, no. 13, pp. 4863-4868. https://doi.org/10.1073/pnas.1116478109