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Discover resources for the Talos 12 TEM
The Thermo Scientific Talos 12 TEM is the next step in powerful TEM and STEM 2D imaging and tomography for 3D visualization. With a modular design, it can be configured for routine TEM imaging of cells and tissues for research and pathology, sample characterization with different STEM and EDS detectors, or as an entry-level cryo-TEM for structural biology research from negative stain imaging to biochemical optimization and data collection for cryo-EM single particle analysis.
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Researchers using the Talos TEM
Ultrastructural cellular imaging in virology research
Dr. Melina Vallbracht is a Group Leader and Head of Microscopy at the Paul-Ehrlich-Institute, Germany. Dr. Vallbracht’s team works to understand how the Ebola virus and other negative-strand RNA viruses remodel the host cell to replicate and create new virions.
In M. Vallbracht et al., she explored how the Ebola virus replicates in membraneless organelles termed viral factories (VFs).
In the example below, the Talos TEM was used to examine thin sections of cells infected with Ebola and illustrates virus nucleocapsid formation over time. The full study illustrates a more complete picture of Ebola nucleocapsid assembly that drives viral factory maturation.
Dr. Melina Vallbracht uses the Talos TEM for ultrastructural investigations of Ebola-infected cells.
Adapted from Dr. Vallbracht's study, thin-section transmission electron microscopy of Ebola viral factories. At 22 hours post-infection, the assembled nucleocapsids appear in parallel bundles (A, B), dispersed throughout the cytoplasm, later separating on the way to the budding sites at the plasma membrane (C). Plasma membrane ruffling (D) is also observed during later stages of infection. Learn more in the full article: Vallbracht, M., et al. Nucleocapsid assembly drives Ebola viral factory maturation and dispersion. Cell 188(3) (2025). doi: 10.1016/j.cell.2024.11.024
Structural biology of neurotoxins
Prof. Dr. Christos Gatsogiannis is a Principal Investigator at the University of Muenster, Germany. His team elucidates the architecture of complex nanomachines using structural biology techniques. One of their research areas examines the molecular mechanisms of pore-forming neurotoxins.
In B.U. Klink, et al., his team use cryo-EM to uncover the structural mechanism for how the α-LTX toxin in black widow spider venom inserts itself into presynaptic nerve terminals and triggers a massive release of neurotransmitters. In this work, negative stain imaging with the Talos TEM was used to optimize sample preparation and investigate the membrane incorporation of the α-LTX toxin into liposomes.
Prof. Dr. Christos Gatsogiannis uses the Talos TEM for his structural biology studies of neurotoxins.
Adapted from Prof. Dr. Gatsogiannis's study, structural characterization of black widow spider venom. (A) Negative stain images of latrotoxin tetramer pores on liposomes, shown across six representative fields. (B) From 988 micrographs, a total of 108 similar particles were used to create a 2D class average. The individual domains of the toxin are highlighted (CD - connector domain, HBD helical bundle domain, PD beta-sheet plug domain, ARD - ankyrin repeat domain). (C) Molecular model of the complete α-LTX pore obtained by combining data from cryo-EM and the AlphaFold2 prediction (not shown) overlaid in the negative stain average of the α-LTX pore on liposomes. Learn more in the full article: Klink, B.U., et al. Structural basis of α-latrotoxin transition to a cation-selective pore. Nat Commun 15, 8551 (2024). https://doi.org/10.1038/s41467-024-52635-5
Talos 12 TEM documents
For Research Use Only. Not for use in diagnostic procedures.