# TFS Talos-L120C, a 120kV transmission electron microscope for structural studies

> **NIH NIH S10** · VANDERBILT UNIVERSITY · 2024 · $656,315

## Abstract

Structural investigation of biological complexes at near atomic resolution is essential to illuminating the molecular
mechanism of biological systems under physiological and pathological conditions; these efforts ultimately lead
to developing therapeutics and improving human health. Understanding lipid-protein interactions, protein-ligand
interactions, multi-subunit protein assembly, and physiologically relevant conformational ensembles require
experimental measurement and structural determination, because these are questions too complex to solve in
silico even with today’s most advanced structural prediction and simulation software. Single particle analysis
(SPA) cryo-EM is used extensively for structural determination at Vanderbilt investigators to illuminate novel
mechanism underlying DNA replication (Chazin and Eichman), nuclear export of mRNAs (Ren), calcium
signaling (Karakas), host-pathogen interaction (Cover, Crowe, Lacy, and Wan), therapeutic antibody
development (Crowe), membrane trafficking (Jackson), neuronal signaling (Nakagawa and Zhou), biomimetic
polymers (Duvall), energy homeostasis (Lepesheva), and membrane protein biology of GPCR, ion channels,
and transporters (Hamm, Karakas, and Nakagawa). Furthermore, technological advance in cryo-electron
tomography enabled visualization of macromolecules in subcellular compartments in situ, providing access to
intact ultrastructure of synapses (Zhou) and viral assembly mechanism in host cells (Wan). Essential to these
discoveries are the extensive trial-and-error efforts to optimize and identify specimens most suitable for high
resolution analysis using the state-of-the-art Titan Krios. This process is often referred to as specimen screening,
which requires visualization of negative stain specimen by a 100-200kV transmission electron microscope (TEM)
equipped with a detector suitable for image acquisition and subsequent data processing to address specimen
quality. We have been extensively using two old TEMs equipped with outdated technologies, 100kV Morgagni
and 200kV Tecnai-F20 (TF20), for screening. However, all components of Morgagni and the detector of TF20
are out of replacement parts. Adding a modern detector to TF20 will not add usage hours, yet be prohibitively
costly. Considering the low cost-benefit of upgrading TF20 and our inability to repair the Morgagni, we propose
to retire the two old TEMs and acquire the modern 120kV TEM, Talos L120C, as a replacement. Talos L120C
will provide additional ability to image vitrified samples at cryogenic temperatures in the instance where our cryo-
TEM Glacios, used for screening vitrified specimen, is temporarily down for repair. Collectively, the Talos L120C,
which will be housed in the cryo-EM core facility and used by the investigators from four Schools and Colleges
at Vanderbilt, will fulfill the needs currently met by the retiring TEMs and further establish a robust cryo-EM
workflow pipeline to advance the NIH funded projects aimed to i...

## Key facts

- **NIH application ID:** 10852499
- **Project number:** 1S10OD036307-01
- **Recipient organization:** VANDERBILT UNIVERSITY
- **Principal Investigator:** Terunaga Nakagawa
- **Activity code:** S10 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2024
- **Award amount:** $656,315
- **Award type:** 1
- **Project period:** 2024-09-01 → 2025-08-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/10852499

## Citation

> US National Institutes of Health, RePORTER application 10852499, TFS Talos-L120C, a 120kV transmission electron microscope for structural studies (1S10OD036307-01). Retrieved via AI Analytics 2026-05-26 from https://api.ai-analytics.org/grant/nih/10852499. Licensed CC0.

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