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Low-dose images obtained by electron cryo-microscopy (cryo-EM) are often affected by blurring caused by sample motion during electron beam exposure, degrading signal especially at high resolution. We show here that we can align frames of movies, recorded with a direct electron detector during beam exposure of rotavirus double-layered particles, thereby greatly reducing image blurring caused by beam-induced motion and sample stage instabilities. This procedure increases the efficiency of cryo-EM imaging and enhances the resolution obtained in three-dimensional reconstructions of the particle. Using movies in this way is generally applicable to all cryo-EM samples and should also improve the performance of midrange electron microscopes that may have limited mechanical stability and beam coherence.
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http://dx.doi.org/10.1016/j.str.2012.08.026 | DOI Listing |
Mol Cell Proteomics
September 2025
Institute of Biotechnology, HiLIFE, Faculty of Medicine, University of Helsinki, Helsinki, Finland. Electronic address:
Structural proteomics has undergone a profound transformation, driven by the convergence of advanced experimental methodologies and computational innovations. Cutting-edge mass spectrometry (MS)-based approaches, including cross-linking MS (XL-MS), hydrogen-deuterium exchange MS (HDX-MS), and limited proteolysis MS (LiP-MS), now enable unprecedented insights into protein topology, conformational dynamics, and protein-protein interactions. These methods, complemented by affinity purification (AP), co-immunoprecipitation (co-IP), proximity labeling (PL), and spatial proteomics techniques, have expanded our ability to characterize the structural proteome at a systems-wide scale.
View Article and Find Full Text PDFMicrosc Res Tech
September 2025
Center for Optical Technologies, Aalen University, Aalen, Germany.
Understanding the intracellular fate of nanoparticles (NPs) is essential for advancing nanomedicine, particularly in targeted drug delivery for cancer therapy. Here, we present a complementary cryogenic microscopy workflow across scales to investigate the uptake and subcellular localization of zirconyl-containing inorganic-organic hybrid nanoparticles (IOH-NPs) in murine breast cancer cells. Our approach integrates cryogenic fluorescence microscopy (cryo-FM), cryo-focused ion beam scanning electron microscopy (cryo-FIBSEM), and cryo-soft X-ray tomography (cryo-SXT), enabling molecular specificity, high-resolution imaging, and volumetric ultrastructural analysis in near-native cellular states.
View Article and Find Full Text PDFJ Am Chem Soc
August 2025
Department of Materials, Imperial College London, South Kensington, London SW7 2AZ, U.K.
Although the Haber-Bosch process for industrial ammonia production is hailed by many as one of the most influential breakthroughs of the 20th century, its decarbonization and decentralization remain a critical challenge. One of the most promising and fast improving approaches is electrochemical nitrogen reduction mediated by lithium. However, the impact of electrolyte configuration on the formation of the solid electrolyte interphase (SEI) and its effect on selective nitrogen reduction is still elusive.
View Article and Find Full Text PDFCell Rep
August 2025
de Duve Institute, UCLouvain, 1200 Brussels, Belgium; WELBIO Department, WEL Research Institute, 1300 Wavre, Belgium. Electronic address:
Transforming growth factor β1 (TGF-β1) is an immunosuppressive cytokine produced as a latent homodimer, in which mature TGF-β1 is encapsulated and kept inactive by the latency-associated peptide (LAP). The transmembrane protein GARP presents latent TGF-β1 on the surface of regulatory T cells (Tregs) to enable activation and release of mature TGF-β1 by integrins. Here, we derived monoclonal antibodies (mAbs) that activate latent TGF-β1 anchored on cells by a transmembrane protein.
View Article and Find Full Text PDFNat Commun
July 2025
VIB Center for Medical Biotechnology, VIB, Ghent, Belgium.
Influenza B viruses are antigenically diverse and contribute significantly to the annual influenza burden. Here we report influenza B virus neutralizing single-domain antibodies that target highly conserved regions of the hemagglutinin and neuraminidase. Structural studies by single particle electron cryo-microscopy (cryo-EM) revealed that one of these single-domain antibodies prevents the conformational transition of the viral hemagglutinin to the post-fusion state by targeting a quaternary epitope spanning two protomers in the hemagglutinin-stem region.
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