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Electron Microscopy Solutions
Transmission Electron Microscopes

Talos F200C TEM for Life Sciences

Industry-leading power and versatility for 3D imaging of molecules and cells

The Thermo Scientific™ Talos™ F200C transmission electron microscope (TEM) is a powerful, versatile system for delivering 3D characterization of biological and biomaterials samples in cell biology, structural biology, and nanotechnology research. With its innovative design to increase throughput, stability, and ease of use, the Talos F200C TEM enables scientists to quickly obtain better insight and understanding of macromolecular structures, cellular components, cells, and tissues in three dimensions.




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High Resolution for 3D Insight

The Talos F200C TEM’s constant-power, C-TWIN lens delivers outstanding optical performance to help ensure an optimal balance between contrast and resolution.

Talos F200C TEM Benefits for Life Science

Support a wide range of users. The Talos F200C TEM enables a wider range of users to access powerful 3D characterization capabilities for biological and biomaterials samples with a fully digital interface, class-leading ergonomics, and remote control features.
Get results faster. Extended automation combined with a fully integrated 16-Megapixel CMOS detector reduces the number of required steps.
Improve repeatability and reliability. A constant-power objective lens, (optional) Piezo stage, highly stable optics, and a robust system enclosure deliver maximum system stability.
Do more on one system. Perform the widest range of applications from a single platform.


 

Featured Document

Talos F200C TEM Datasheet

The Talos F200C is a 200kV Transmission Electron Microscope (TEM), designed for cryo and room temperature applications. It supports multiple automated imaging applications, such as tomography and single particle analysis (SPA), on both vitrified and ambient suspensions, cell organelles, and cells.

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Publication list for Talos for Life Sciences

Title: Lis1 has two opposing modes of regulating cytoplasmic dynein
Authors: DeSantis, M.E., Cianfrocco, M.A., Htet, Z.M., Tran, P.T., Reck-Peterson, S.L. and Leschziner, A.E.  Department of Cellular and Molecular Medicine, University of California San Diego, La Jolla CA, 92093, USA.  
References: bioRxiv (2017) 
DOI10.1016/j.cell.2017.08.037
Date: June 2017
Abstract
Title: Lis1 has two opposing modes of regulating cytoplasmic dynein
Authors: DeSantis, M.E., Cianfrocco, M.A., Htet, Z.M., Tran, P.T., Reck-Peterson, S.L. and Leschziner, A.E.  Department of Cellular and Molecular Medicine, University of California San Diego, La Jolla CA, 92093, USA.  
References: bioRxiv (2017) 
DOI10.1016/j.cell.2017.08.037
Date: June 2017
Abstract: Regulation is central to the functional versatility of cytoplasmic dynein, a motor involved in intracellular transport, cell division, and neurodevelopment. Previous work established that Lis1, a conserved and ubiquitous regulator of dynein, binds to its motor domain and induces a tight microtubule-binding state in dynein. The work we present here - a combination of biochemistry, single-molecule assays, cryo-electron microscopy and in vivo experiments - led to the surprising discovery that Lis1 has two opposing modes of regulating dynein, being capable of inducing both low and high affinity for the microtubule. We show that these opposing modes depend on the stoichiometry of Lis1 binding to dynein and that this stoichiometry is regulated by the nucleotide state of dynein's AAA3 domain. We present data on the in vitro and in vivo consequences of abolishing the novel Lis1-induced weak microtubule-binding state in dynein and propose a new model for the regulation of dynein by Lis1.  Comments: open access, pre-print, non-peer reviewed (all rights reserved); FEI Vitrobot; FEI Talos Arctica, Gatan K2 Summit, Leginon (superresolution mode)
Title: Achieving Better Than 3 Å Resolution By Single Particle Cryo-EM At 200 keV
Authors: Herzik, M.A., Wu, M. and Lander, G.C.  Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California 92037, USA  
References: bioRxiv (2017) 
DOI10.1101/141994
Date: May 2017
Abstract
Title: Achieving Better Than 3 Å Resolution By Single Particle Cryo-EM At 200 keV
Authors: Herzik, M.A., Wu, M. and Lander, G.C.  Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California 92037, USA  
References: bioRxiv (2017) 
DOI10.1101/141994
Date: May 2017
Abstract: Technical and methodological advances in single-particle cryo-electron microscopy (cryo-EM) have expanded the technique into a resolution regime that was previously only attainable by X-ray crystallography. Although single-particle cryo-EM has proven to be a useful technique for determining the structures of biomedically relevant molecules at near-atomic resolution, nearly 98% of the structures resolved to better than 4 Å resolution have been determined using 300 keV transmission electron microscopes (TEMs). We demonstrate that it is possible to obtain cryo-EM reconstructions of macromolecular complexes at a range of sizes to better than 3 Å resolution using a 200 keV TEM. These structures are of sufficient quality to unambiguously assign amino acid rotameric conformations and identify ordered water molecules, features previously thought only to be resolvable using TEMs operating at 300 keV.  Comments: open access (CC BY 4.0), preprint, non-peer reviewed; FEI Talos Arctica, Gatan K2 Summit, Leginon