Please use this identifier to cite or link to this item: doi:10.22028/D291-28961
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Title: Merging In-Solution X-ray and Neutron Scattering Data Allows Fine Structural Analysis of Membrane-Protein Detergent Complexes
Author(s): Dias Mirandela, Gaëtan
Tamburrino, Giulia
Ivanović, Miloš T
Strnad, Felix M
Byron, Olwyn
Rasmussen, Tim
Hoskisson, Paul A
Hub, Jochen Sebastian
Zachariae, Ulrich
Gabel, Frank
Javelle, Arnaud
Language: English
Title: The journal of physical chemistry letters
Volume: 9
Issue: 14
Startpage: 3910
Endpage: 3914
Publisher/Platform: American Chemical Society (ACS)
Year of Publication: 2018
Publikation type: Journal Article
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.
DOI of the first publication: 10.1021/acs.jpclett.8b01598
Link to this record: hdl:20.500.11880/27785
ISSN: 1948-7185
Date of registration: 17-Sep-2019
Faculty: NT - Naturwissenschaftlich- Technische Fakultät
Department: NT - Physik
Professorship: NT - Prof. Dr. Jochen Hub
Collections:SciDok - Der Wissenschaftsserver der Universität des Saarlandes

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