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Instruments / Technical Area	Publication Details	Published	Actions
B21-High Throughput SAXS	Merging in-solution x-ray and neutron scattering data allows fine structural analysis of membrane–protein detergent complexes Gaetan Dias Mirandela , Giulia Tamburrino , Miloš T. Ivanović , Felix M. Strnad , Olwyn Byron , Tim Rasmussen , Paul A. Hoskisson , Jochen S. Hub , Ulrich Zachariae , Frank Gabel , Arnaud Javelle The Journal Of Physical Chemistry Letters DOI: 10.1021/acs.jpclett.8b01598 Diamond Proposal Number(s): [15616] Open Access Show Abstract ▼ 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.	Jul 2018
Krios I-Titan Krios I at Diamond	Structure of the MacAB–TolC ABC-type tripartite multidrug efflux pump Anthony Fitzpatrick , Salomé Llabrés , Arthur Neuberger , James N. Blaza , Xiao-Chen Bai , Ui Okada , Satoshi Murakami , Hendrik W. Van Veen , Ulrich Zachariae , Sjors H. W. Scheres , Ben F. Luisi , Dijun Du Nature Microbiology 2 DOI: 10.1038/nmicrobiol.2017.70 Show Abstract ▼ Abstract: The MacA–MacB–TolC assembly of Escherichia coli is a transmembrane machine that spans the cell envelope and actively extrudes substrates, including macrolide antibiotics and polypeptide virulence factors. These transport processes are energized by the ATPase MacB, a member of the ATP-binding cassette (ABC) superfamily. We present an electron cryo-microscopy structure of the ABC-type tripartite assembly at near-atomic resolution. A hexamer of the periplasmic protein MacA bridges between a TolC trimer in the outer membrane and a MacB dimer in the inner membrane, generating a quaternary structure with a central channel for substrate translocation. A gating ring found in MacA is proposed to act as a one-way valve in substrate transport. The MacB structure features an atypical transmembrane domain with a closely packed dimer interface and a periplasmic opening that is the likely portal for substrate entry from the periplasm, with subsequent displacement through an allosteric transport mechanism.	May 2017

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