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Updated: Feb 25, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Sample Preparation for Membrane Protein Structural Studies by Solid-State NMR
Denis Lacabanne1, Britta Kunert1, Carole Gardiennet1,2
1Molecular Microbiology and Structural Biochemistry, Labex Ecofect, UMR 5086 CNRS - Université de Lyon, 7 Passage du Vercors, 69367, Lyon, France.
Abstract:
Conformational studies of membrane proteins remain a challenge in the field of structural biology, and in particular the investigation of the proteins in a native-like lipid environment. Solid-state NMR presents a valuable opportunity for this, and we present here three critical steps in the solid-state NMR sample preparation, i.e., membrane reconstitution of the protein in native lipids, rotor filling, and sample quality assessment, at the example of the Bacillus subtilis ATP-binding cassette transporter BmrA.

