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Updated: Feb 6, 2026

gP2S, an Information Management System for CryoEM Experiments
Published on: June 10, 2021
Advances in cryoEM and its impact on β-pore forming proteins
Courtney M Boyd1, Doryen Bubeck1
1Department of Life Sciences, Imperial College London, South Kensington Campus, London SW7 2AZ, UK.
Abstract:
Deployed by both hosts and pathogens, β-pore-forming proteins (β-PFPs) rupture membranes and lyse target cells. Soluble protein monomers oligomerize on the lipid bilayer where they undergo dramatic structural rearrangements, resulting in a transmembrane β-barrel pore. Advances in electron cryo-microscopy (cryoEM) sample preparation, image detection, and computational algorithms have led to a number of recent structures that reveal a molecular mechanism of pore formation in atomic detail.
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