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Springer (part of Springer Nature), Journal of Biomolecular NMR, 2(62), p. 199-208

DOI: 10.1007/s10858-015-9936-5

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Efficient cellular solid-state NMR of membrane proteins by targeted protein labeling

Journal article published in 2015 by Lindsay A. Baker, Mark Daniëls, Elwin A. W. van der Cruijsen, Gert E. Folkers ORCID, Marc Baldus
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

Solid-state NMR spectroscopy (ssNMR) has made significant progress towards the study of membrane proteins in their native cellular membranes. However, reduced spectroscopic sensitivity and high background signal levels can complicate these experiments. Here, we describe a method for ssNMR to specifically label a single protein by repressing endogenous protein expression with rifampicin. Our results demonstrate that treatment of E. coli with rifampicin during induction of recombinant membrane protein expression reduces background signals for different expression levels and improves sensitivity in cellular membrane samples. Further, the method reduces the amount of time and resources needed to produce membrane protein samples, enabling new strategies for studying challenging membrane proteins by ssNMR.