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Instruments / Technical Area	Publication Details	Published	Actions
Krios I-Titan Krios I at Diamond	Distance tuneable integral membrane protein containing floating bilayers via in situ directed self-assembly Stephen C. L. Hall , David J. Hardy , Eilis C. Bragginton , Hannah Johnston , Tudor Onose , Rachel Holyfield , Pooja Sridhar , Timothy J. Knowles , Luke A. Clifton Nanoscale 277 DOI: 10.1039/D3NR04622B Diamond Proposal Number(s): [33797] Open Access Show Abstract ▼ Abstract: Model membranes allow for structural and biophysical studies on membrane biochemistry at the molecular level, albeit on systems of reduced complexity which can limit biological accuracy. Floating supported bilayers offer a means of producing planar lipid membrane models not adhered to a surface, which allows for improved accuracy compared to other model membranes. Here we communicate the incorporation of an integral membrane protein complex, the multidomain β-barrel assembly machinery (Bam), into our recently developed in situ self-assembled floating supported bilayers. Using neutron reflectometry and quartz crystal microbalance measurements we show this sample system can be fabricated using a two-step self-assembly process. We then demonstrate the complexity of the model membrane and tuneability of the membrane-to-surface distance using changes in the salt concentration of the bulk solution. Results demonstrate an easily fabricated, biologically accurate and tuneable membrane assay system which can be utilized for studies on integral membrane proteins within their native lipid matrix.	Jun 2024
I04-Macromolecular Crystallography	An octameric PqiC toroid stabilises the outer-membrane interaction of the PqiABC transport system Benjamin F. Cooper , Giedrė Ratkevičiūtė , Luke A. Clifton , Hannah Johnston , Rachel Holyfield , David J. Hardy , Simon G. Caulton , William Chatterton , Pooja Sridhar , Peter Wotherspoon , Gareth W. Hughes , Stephen C. L. Hall , Andrew L. Lovering , Timothy J. Knowles Embo Reports 68 DOI: 10.1038/s44319-023-00014-4 Diamond Proposal Number(s): [26803] Open Access Show Abstract ▼ Abstract: The E. coli Paraquat Inducible (Pqi) Pathway is a putative Gram-negative phospholipid transport system. The pathway comprises three components: an integral inner membrane protein (PqiA), a periplasmic spanning MCE family protein (PqiB) and an outer membrane lipoprotein (PqiC). Interactions between all complex components, including stoichiometry, remain uncharacterised; nevertheless, once assembled into their quaternary complex, the trio of Pqi proteins are anticipated to provide a continuous channel between the inner and outer membranes of diderms. Here, we present X-ray structures of both the native and a truncated, soluble construct of the PqiC lipoprotein, providing insight into its biological assembly, and utilise neutron reflectometry to characterise the nature of the PqiB-PqiC-membrane interaction. Finally, we employ phenotypic complementation assays to probe specific PqiC residues, which imply the interaction between PqiB and PqiC is less intimate than previously anticipated.	Jan 2024

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