Tomo software

Manufactured by Thermo Fisher Scientific

Tomo software is a digital imaging and analysis platform developed by Thermo Fisher Scientific. The core function of Tomo software is to capture, process, and analyze images across various scientific applications.

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Lab products found in correlation

Titan krios microscope, by Ametek (1 mentions) K2 direct electron detector, by Ametek (1 mentions) Falcon 3 direct electron detector, by Thermo Fisher Scientific (1 mentions) Talos arctica, by Thermo Fisher Scientific (1 mentions) Bioquantum, by Ametek (1 mentions) K2 summit, by Ametek (1 mentions)

2 protocols using tomo software

Cryo-EM Data Collection Protocols

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Single particle cryoEM data were collected on a Titan Krios microscope (‘Titan Krios 1’ at the Astbury Biostructure Laboratory) operating at 300 kV and Falcon III direct electron detector (Thermo Fisher Scientific) operating in integrating mode. Data were collected using EPU software with parameters as in Supplementary Table 1, based on a published protocol^{34 (link)}. Where the sample was tilted during collection, the autofocus and drift measurements were taken in line with the tilt axis.
Tilt series data were collected using a Titan Krios microscope (‘Titan Krios 2’) operating at 300 kV and Bioquantum energy filter (20 eV) K2 direct electron detector (Gatan) operating in counting mode, using Tomo software (Thermo Fisher Scientific). Data were collected with parameters as in Supplementary Table 2.

Byrne M.J., Iadanza M.G., Perez M.A., Maskell D.P., George R.M., Hesketh E.L., Beales P.A., Zack M.D., Berry C, & Thompson R.F. (2021). Cryo-EM structures of an insecticidal Bt toxin reveal its mechanism of action on the membrane. Nature Communications, 12, 2791.

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Cryo-EM Tilt-Series Imaging Protocol

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Tilt-series were acquired on a Talos Arctica (Thermo Fisher Scientific) operated at 200 kV in parallel beam condition, a K2 Summit direct electron detector, and a BioQuantum energy filter (Gatan Inc.) operated in zero-loss mode with a slit width of 20 eV. Data were collected using Tomo software (Thermo Fisher Scientific), at a nominal magnification of 63,000× with a calibrated pixel size of 2.8 Å and between −5 and −8 µm defocus. Tilt series were acquired following the dose symmetric scheme between +60° and −60° with a step size of 2° (58 (link)). Each tilt image was acquired in electron counting mode with a total dose of 70 e⁻/A².

Moreaud L., Viollet S., Urvoas A., Valerio-Lepiniec M., Mesneau A., Li de la Sierra-Gallay I., Miller J., Ouldali M., Marcelot C., Balor S., Soldan V., Meriadec C., Artzner F., Dujardin E, & Minard P. (2023). Design, synthesis, and characterization of protein origami based on self-assembly of a brick and staple artificial protein pair. Proceedings of the National Academy of Sciences of the United States of America, 120(11), e2218428120.

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