Summary
X-ray crystallography is the field of structural biology to which, to date, amphipols have contributed the least. Complexes formed from a membrane protein (MP) and the best characterized amphipol, A8-35, have stubbornly refused to crystallize, whereas ternary MP/A8-35/detergent complexes yielded crystals diffracting to low resolution. Plausible causes of these difficulties and possible ways to alleviate them will be discussed in relation to solution measurements and other data. New tools are being developed, including more adequate amphipols. An alternative approach relying on the use of amphipols to deliver membrane proteins to a lipidic mesophase, where they do crystallize, has been explored with very promising results.
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Popot, JL. (2018). Amphipols and Membrane Protein Crystallization. In: Membrane Proteins in Aqueous Solutions. Biological and Medical Physics, Biomedical Engineering. Springer, Cham. https://doi.org/10.1007/978-3-319-73148-3_11
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