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Instruments / Technical Area	Publication Details	Published	Actions
Krios I-Titan Krios I at Diamond Krios II-Titan Krios II at Diamond Krios III-Titan Krios III at Diamond Krios IV-Titan Krios IV at Diamond Krios V-Titan Krios V at Diamond	Coming clean and avoiding bubble trouble - using detergents wisely in the purification of membrane proteins for Cryo-EM studies Bowen Chen , Peter Harrison , Vasileios Kargas , Naomi Pollock , Robert C. Ford , Stephen M. Prince , Richard F. Collins Biomolecules 15 DOI: 10.3390/biom15091315 Diamond Proposal Number(s): [29255, 36408, 27436, 33941] Open Access Show Abstract ▼ Abstract: Detergent solubilisation remains the most commonly used but potentially problematic method to extract membrane proteins from lipid bilayers for Cryo-EM studies. Although recent advances have introduced excellent alternatives—such as amphipols, nanodiscs and SMALPs—the use of detergents is often necessary for intermediate steps. In this paper, we share our experiences working with detergent-solubilised samples within the modern Cryo-EM structural pipeline from the perspective of an EM specialist. Our aim is to inform novice users about potential challenges they may encounter. Drawing on specific examples from a variety of biological membrane systems, including Magnesium channels, lipopolysaccharide biosynthesis, and the human major facilitator superfamily transporters, we describe how the intrinsic properties of detergent-extracted samples can affect protein purification, Cryo-EM grid preparation (including the formation of vitreous ice) and the reconstitution of proteins into micelles. We also discuss how these unique characteristics can impact different stages of structural analysis and lead to complications in single-particle averaging software analysis. For each case, we present our insights into the underlying causes and suggest possible mitigations or alternative approaches.	Sep 2025
B21-High Throughput SAXS	Nano-encapsulated Escherichia coli divisome anchor ZipA, and in complex with FtsZ Sarah C. Lee , Richard Collins , Yu-Pin Lin , Mohammed Jamshad , Claire Broughton , Sarah A. Harris , Benjamin S. Hanson , Cecilia Tognoloni , Rosemary A. Parslow , Ann E. Terry , Alison Rodger , Corinne J. Smith , Karen J. Edler , Robert Ford , David I. Roper , Timothy R. Dafforn Scientific Reports 9 DOI: 10.1038/s41598-019-54999-x Diamond Proposal Number(s): [9727] Open Access Show Abstract ▼ Abstract: The E. coli membrane protein ZipA, binds to the tubulin homologue FtsZ, in the early stage of cell division. We isolated ZipA in a Styrene Maleic Acid lipid particle (SMALP) preserving its position and integrity with native E. coli membrane lipids. Direct binding of ZipA to FtsZ is demonstrated, including FtsZ fibre bundles decorated with ZipA. Using Cryo-Electron Microscopy, small-angle X-ray and neutron scattering, we determine the encapsulated-ZipA structure in isolation, and in complex with FtsZ to a resolution of 1.6 nm. Three regions can be identified from the structure which correspond to, SMALP encapsulated membrane and ZipA transmembrane helix, a separate short compact tether, and ZipA globular head which binds FtsZ. The complex extends 12 nm from the membrane in a compact structure, supported by mesoscale modelling techniques, measuring the movement and stiffness of the regions within ZipA provides molecular scale analysis and visualisation of the early divisome.	Dec 2019

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