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Transmission Electron Microscopes

Talos Arctica TEM for Life Sciences

Resolve 3D macromolecular structures quickly, efficiently, and accurately

The Thermo Scientific™ Talos™ Arctica is a 200kV FEG transmission and scanning electron microscope (S/TEM). It is a powerful, stable, and versatile system for delivering high-resolution 3D characterization of biological and biomaterials samples in cell biology, structural biology, and nanotechnology research. The Talos S/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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Fastest 200 kV FEG S/TEM for sample analysis in multiple dimensions 

The Talos TEM is a new generation in TEM, built to deliver rapid access to 2D and 3D data so that you can concentrate on discovery. The system's constant-power, C-Twin lens delivers outstanding optical performance to ensure an optimal balance of contrast and resolution. The Talos TEM's ultra-stable platform includes a piezo stage with stable electronics and a rugged system enclosure for maximum thermal and mechanical stability.

Talos Arctica TEM Benefits for Structural Biology

Increased data acquisition speed: Acquisition speeds have been improved up to 3 times for tomography and up to 1.5 times for single particle analysis when EPU is used compared to side entry loading systems
High data throughput: Robotic sample handling and automated loading for up to 12 samples enhances up to 40% in data throughput
Unattended operation: Autofilling of liquid nitrogen and powerful applications SW allows for continuous unattended platform operation and automated data acquisition
Low cost of ownership: New design allows for remote diagnostics and preventive service, lowering ownership cost and maximizing systems uptime.

Featured News

Congratulations to the winners of the 2017 Nobel Prize in Chemistry.

Three scientists; Dr. Jacques Dubochet Dr. Joachim Frank, and Dr. Richard Henderson, were awarded the prize for their developments within Cryo-Electron Microscopy.

We are extremely proud of what these researchers and the structural biology community have achieved.

2017 Young Investigator Award

Have you recently published your work in a scientific journal? Does your work possess significant biological relevance and/or seriously impact the research community? You might be able to win $3,000 and a sponsored talk on your subject. Submit your work for the 2017 Thermo Fisher Scientific Young Investigator Life Sciences Award.

Learn more

Featured Document

Talos Arctica STEM Datasheet

The Talos Arctica is a 200 kV FEG Transmission and Scanning Transmission Electron Microscope (S/TEM). It is a powerful, stable, and highly automated system optimized for high-resolution 3D imaging of proteins and macromolecular assemblies as well as high-resolution cellular tomography.

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Publication list for Talos Arctica 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