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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.

Original publication




Journal article


Journal of biomolecular NMR

Publication Date





199 - 208


NMR Spectroscopy, Department of Chemistry, Faculty of Science, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands.


Streptomyces lividans, Escherichia coli, Rifampin, Proteolipids, Bacterial Proteins, Escherichia coli Proteins, Membrane Transport Proteins, Potassium Channels, Recombinant Proteins, Nuclear Magnetic Resonance, Biomolecular, Sensitivity and Specificity, Cloning, Molecular, Protein Conformation