Probing a cell-embedded megadalton protein complex by DNP-supported solid-state NMR

M. Kaplan; Abhishek Cukkemane; Gydo C P Van Zundert; Siddarth Narasimhan; Mark Daniëls; Deni Mance; Gabriel Waksman; Alexandre M J J Bonvin; Rémi Fronzes; Gert E. Folkers; Marc Baldus

doi:10.1038/nmeth.3406

Probing a cell-embedded megadalton protein complex by DNP-supported solid-state NMR

M. Kaplan, Abhishek Cukkemane, Gydo C P Van Zundert, Siddarth Narasimhan, Mark Daniëls, Deni Mance, Gabriel Waksman, Alexandre M J J Bonvin, Rémi Fronzes, Gert E. Folkers^*, Marc Baldus

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

Studying biomolecules at atomic resolution in their native environment is the ultimate aim of structural biology. We investigated the bacterial type IV secretion system core complex (T4SScc) by cellular dynamic nuclear polarization-based solid-state nuclear magnetic resonance spectroscopy to validate a structural model previously generated by combining in vitro and in silico data. Our results indicate that T4SScc is well folded in the cellular setting, revealing protein regions that had been elusive when studied in vitro.

Original language	English
Pages (from-to)	649-652
Number of pages	4
Journal	Nature Methods
Volume	12
Issue number	7
DOIs	https://doi.org/10.1038/nmeth.3406
Publication status	Published - 30 Jun 2015

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title = "Probing a cell-embedded megadalton protein complex by DNP-supported solid-state NMR",

abstract = "Studying biomolecules at atomic resolution in their native environment is the ultimate aim of structural biology. We investigated the bacterial type IV secretion system core complex (T4SScc) by cellular dynamic nuclear polarization-based solid-state nuclear magnetic resonance spectroscopy to validate a structural model previously generated by combining in vitro and in silico data. Our results indicate that T4SScc is well folded in the cellular setting, revealing protein regions that had been elusive when studied in vitro.",

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AU - Kaplan, M.

AU - Cukkemane, Abhishek

AU - Van Zundert, Gydo C P

AU - Narasimhan, Siddarth

AU - Daniëls, Mark

AU - Mance, Deni

AU - Waksman, Gabriel

AU - Bonvin, Alexandre M J J

AU - Fronzes, Rémi

AU - Folkers, Gert E.

AU - Baldus, Marc

PY - 2015/6/30

Y1 - 2015/6/30

N2 - Studying biomolecules at atomic resolution in their native environment is the ultimate aim of structural biology. We investigated the bacterial type IV secretion system core complex (T4SScc) by cellular dynamic nuclear polarization-based solid-state nuclear magnetic resonance spectroscopy to validate a structural model previously generated by combining in vitro and in silico data. Our results indicate that T4SScc is well folded in the cellular setting, revealing protein regions that had been elusive when studied in vitro.

AB - Studying biomolecules at atomic resolution in their native environment is the ultimate aim of structural biology. We investigated the bacterial type IV secretion system core complex (T4SScc) by cellular dynamic nuclear polarization-based solid-state nuclear magnetic resonance spectroscopy to validate a structural model previously generated by combining in vitro and in silico data. Our results indicate that T4SScc is well folded in the cellular setting, revealing protein regions that had been elusive when studied in vitro.

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JO - Nature Methods

JF - Nature Methods

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ER -

Probing a cell-embedded megadalton protein complex by DNP-supported solid-state NMR

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