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.
CITATION STYLE
Lacabanne, D., Kunert, B., Gardiennet, C., Meier, B. H., & Böckmann, A. (2017). Sample preparation for membrane protein structural studies by solid-state NMR. In Methods in Molecular Biology (Vol. 1635, pp. 345–358). Humana Press Inc. https://doi.org/10.1007/978-1-4939-7151-0_19
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