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Chem Phys Lipids. 2019 Jul;221:114-119. doi: 10.1016/j.chemphyslip.2019.03.007. Epub 2019 Mar 30.

Single-particle cryo-EM studies of transmembrane proteins in SMA copolymer nanodiscs.

Author information

1
Department of Biochemistry, University of Illinois, 600 S. Mathews Street, Urbana, IL 61801, United States. Electronic address: sun.changing@gmail.com.
2
Department of Biochemistry, University of Illinois, 600 S. Mathews Street, Urbana, IL 61801, United States.

Abstract

Styrene-maleic acid (SMA) copolymers can extract membrane proteins from native membranes along with lipids as nanodiscs. Preparation with SMA is fast, cost-effective, and captures the native protein-lipid interactions. On the other hand, cryo-EM has become increasingly successful and efficient for structural determinations of membrane proteins, with biochemical sample preparation often the bottleneck. Three recent cryo-EM studies on the efflux transporter AcrB and the alternative complex III: cyt c oxidase supercomplex have demonstrated the potential of SMA nanodisc samples to yield high-resolution structure information of membrane proteins.

KEYWORDS:

Alternative complex III; Cryo-EM; Lipid-protein interaction; Membrane protein; Multidrug transporter AcrB; Nanodisc; SMA; Styrene-maleic acid copolymer; Triacylated cysteine

PMID:
30940443
PMCID:
PMC6500755
[Available on 2020-07-01]
DOI:
10.1016/j.chemphyslip.2019.03.007

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