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Merging In-Solution X-ray and Neutron Scattering Data Allows Fine Structural Analysis of Membrane–Protein Detergent Complexes

Abstract : In-solution small-angle X-ray and neutron scattering (SAXS/SANS) have become popular methods to characterize the structure of membrane proteins, solubilized by either detergents or nanodiscs. SANS studies of protein-detergent complexes usually require deuterium-labeled proteins or detergents, which in turn often lead to problems in their expression or purification. Here, we report an approach whose novelty is the combined analysis of SAXS and SANS data from an unlabeled membrane protein complex in solution in two complementary ways. First, an explicit atomic analysis, including both protein and detergent molecules, using the program WAXSiS, which has been adapted to predict SANS data. Second, the use of MONSA which allows one to discriminate between detergent head- and tail-groups in an ab initio approach. Our approach is readily applicable to any detergent-solubilized protein and provides more detailed structural information on protein-detergent complexes from unlabeled samples than SAXS or SANS alone.
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https://hal.univ-grenoble-alpes.fr/hal-01990373
Contributeur : Frank Thomas <>
Soumis le : mercredi 23 janvier 2019 - 09:30:20
Dernière modification le : mercredi 15 juillet 2020 - 13:02:04

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Gaëtan Dias Mirandela, Giulia Tamburrino, Miloš Ivanović, Felix Strnad, Olwyn Byron, et al.. Merging In-Solution X-ray and Neutron Scattering Data Allows Fine Structural Analysis of Membrane–Protein Detergent Complexes. Journal of Physical Chemistry Letters, American Chemical Society, 2018, 9 (14), pp.3910-3914. ⟨10.1021/acs.jpclett.8b01598⟩. ⟨hal-01990373⟩

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