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- W4225343792 abstract "Membrane proteins are essential for cellular growth, signalling and homeostasis, making up a large proportion of therapeutic targets. However, the necessity for a solubilising agent to extract them from the membrane creates challenges in their structural and functional study. Although amphipols have been very effective for single-particle electron cryo-microscopy (cryoEM) and mass spectrometry, they rely on initial detergent extraction before exchange into the amphipol environment. Therefore, circumventing this pre-requirement would be a big advantage. Here we use an alternative type of amphipol: a cycloalkane-modified amphiphile polymer (CyclAPol) to extract Escherichia coli AcrB directly from the membrane and demonstrate that the protein can be isolated in a one-step purification with the resultant cryoEM structure achieving 3.2 Å resolution. Together this work shows that cycloalkane amphipols provide a powerful approach for the study of membrane proteins, allowing native extraction and high-resolution structure determination by cryoEM." @default.
- W4225343792 created "2022-05-05" @default.
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- W4225343792 date "2021-11-25" @default.
- W4225343792 modified "2023-10-17" @default.
- W4225343792 title "Cycloalkane-modified amphiphilic polymers provide direct extraction of membrane proteins for CryoEM analysis" @default.
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- W4225343792 doi "https://doi.org/10.1038/s42003-021-02834-3" @default.
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