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Falcon 3ec camera

Manufactured by Thermo Fisher Scientific
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The Falcon 3EC camera is a compact and versatile imaging device designed for a wide range of laboratory applications. It features a high-resolution sensor and advanced image processing capabilities to capture clear and detailed images. The camera is compatible with various microscopy techniques and can be easily integrated into existing laboratory equipment.

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Lab products found in correlation

K3 camera, by Ametek (4 mentions) Titan krios g3i, by Thermo Fisher Scientific (2 mentions) Talos arctica g2, by Thermo Fisher Scientific (2 mentions) Vitrobot system, by Thermo Fisher Scientific (2 mentions) Em gp freeze plunger, by Leica Microsystems (2 mentions) Titan krios electron microscope, by Thermo Fisher Scientific (2 mentions) Vitrobot mark 4, by Thermo Fisher Scientific (2 mentions) Titan krios, by Thermo Fisher Scientific (1 mentions) Titan krios transmission, by Thermo Fisher Scientific (1 mentions) Em gp, by Leica camera (1 mentions)

7 protocols using falcon 3ec camera

1

Structural Characterization of S. enterica WbaP

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Data were collected at the MIT Characterization.nano facility. Optimal freezing conditions were screened using the Vitrobot system (Thermo Scientific). Grids were clipped and screened on a Talos Arctica G2 (Thermo Scientific) equipped with a Falcon 3EC camera (Thermo Scientific). Optimal particles were observed in grid GD5-3, containing 2 mg/mL S. enterica WbaP. Based on these preliminary results, 4,481 movies of SMA30-solubilized S. enterica WbaP were collected on a Titan Krios G3i (Thermo Scientific, Table S1) equipped with a K3 camera (Gatan, Inc). Motion correction, CTF estimation, particle extraction, ab-initio reconstruction, and all refinement were conducted using Cryosparc V4.66 ,67 (link)
Dodge G.J., Anderson A.J., He Y., Liu W., Viner R, & Imperiali B. (2023). Mapping the architecture of the initiating phosphoglycosyl transferase from S. enterica O-antigen biosynthesis in a liponanoparticle. bioRxiv.
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2

Cryo-EM Analysis of S. enterica WbaP

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Data were collected at the MIT Characterization.nano facility. Optimal freezing conditions were screened using the Vitrobot system (Thermo Fisher Scientific). Grids were clipped and screened on a Talos Arctica G2 (Thermo Fisher Scientific) equipped with a Falcon 3EC camera (Thermo Fisher Scientific). Optimal particles were observed in grid GD5-3, containing 2 mg/mL S. enterica WbaP. Based on these preliminary results, 4481 movies of SMA30-solubilized S. enterica WbaP were collected on a Titan Krios G3i (Thermo Fisher Scientific, Supplementary file 1B) equipped with a K3 camera (Gatan, Inc). Motion correction, CTF estimation, particle extraction, ab-initio reconstruction, and all refinement steps were conducted using Cryosparc V4 Punjani, 2020 (link); Punjani et al., 2017 (link).
Dodge G.J., Anderson A.J., He Y., Liu W., Viner R, & Imperiali B. (2024). Mapping the architecture of the initiating phosphoglycosyl transferase from S. enterica O-antigen biosynthesis in a liponanoparticle. eLife, 12, RP91125.
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3

Cryo-EM Imaging of HUWE1N Protein

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4 μL of HUWE1N at 0.8 mg/mL were applied to a Quantifoil R2/2 Cu 200 mesh grid, freshly glow-discharged at 20 mA for 60 s in a SCD 005 Sputter Coater (BAL-TEC). After 1 s pre-blotting time, the sample was blotted for 2 s with a relative humidity of 70% and a temperature of 4°C in an EM GP freeze plunger (Leica Microsystems). Cryo-EM grids were screened using a Glacios equipped with a Falcon3EC camera (Thermo Fisher Scientific). The selected grid was recorded on a Titan Krios electron microscope (ThermoFisher) equipped with a K3 camera (Gatan) in counting mode at the Institute of Science and Technology Austria. The dataset was recorded both untilted and at 25° stage tilt. The microscope was operated in nanoprobe mode with a beam diameter of 1200 nm at a nominal magnification of 105 000x, resulting in a calibrated pixel size of 0.86 Å per pixel. Images were collected in super-resolution. Four images were taken per hole from different non-overlapping areas using image beam shift. The total electron dose of 60 electrons per Å2 (link) was fractionated into 40 frames. A total number of 2580 movies were acquired without tilt, and 1958 movies were acquired at tilt. A defocus range from −2 to −3.5 μm was used.
Grabarczyk D.B., Petrova O.A., Deszcz L., Kurzbauer R., Murphy P., Ahel J., Vogel A., Gogova R., Faas V., Kordic D., Schleiffer A., Meinhart A., Imre R., Lehner A., Neuhold J., Bader G., Stolt-Bergner P., Böttcher J., Wolkerstorfer B., Fischer G., Grishkovskaya I., Haselbach D., Kessler D, & Clausen T. (2021). HUWE1 employs a giant substrate-binding ring to feed and regulate its HECT E3 domain. Nature chemical biology, 17(10), 1084-1092.
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4

Cryo-EM Imaging of PSI-Liposome Fusion

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The PSI was dissolved in a pH 4.5 buffer (27 mM Na-H3PO4 and 140 mM NaCl). A 3-μL aliquot of 100 μM PSI solution was mixed with a 500 μL of liposome solution (5 μM). The liposomes used were 1:1:1 PC/PE/PS. After addition of the PSI, the mixture was incubated for 5 min, followed by quick-freezing in liquid nitrogen to quench the fusion process.
A 4-μl aliquot of the samples was placed on a freshly glow-discharged lacey carbon EM grid. After 2.5 s of blotting with filter paper, the grid was flash-plunged in liquid ethane using a Vitrobot Mark IV (Thermo Fisher Scientific Inc.) at 20 °C and 100% humidity. The samples were imaged in low-dose conditions using a Titan Krios (Thermo Fisher Scientific Inc.) operating at 300 kV. The images of all conditions were collected at a nominal magnification of ×47,000 and an under-focus of 2.0 to 3.0 μm on a Falcon 3EC camera (4096 pixels × 4096 pixels).
Zhao X., Ma X., Dupius J.H., Qi R., Tian J.(., Chen J., Ou X., Qian Z., Liang D., Wang P., Yada R.Y, & Wang S. (2021). Negatively charged phospholipids accelerate the membrane fusion activity of the plant-specific insert domain of an aspartic protease. The Journal of Biological Chemistry, 298(1), 101430.
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5

Transmission Electron Microscopy of Vitrified Samples

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Positively stained samples were examined in a Tecnai F30 G2 (link) transmission electron microscope (Thermo Fisher Scientific) at 300 kV. Electron micrographs at 12,000× or 15,500× magnification were recorded with the Thermo Fisher Scientific software TIA (TEM Imaging & Analysis version 4.15 SP1) or EPU (version 1.11.1.50REL) on a Falcon 3EC camera (Thermo Fisher Scientific) operated in linear mode. High-contrast images were recorded with ~50 e−/pixel total dose and a defocus of –30 to –70 µm.
Vitrified samples were examined in a Titan Krios transmission electron microscope (FEI) at 300 kV with a GATAN GIF Quantum post-column energy filter in zero-loss peak mode. Electron micrographs of lysed yeast cells at 11,500× magnification were recorded with the software SerialEM v3.8.0beta24 on a K2 Summit direct detector (Gatan). Screening images were acquired with a dose of 0.05 e−/Ų and images of spread chromatin with a dose of 0.2 e−/Ų (dose-fractionated) and a defocus of –50 µm. Images of regions of interest within spread chromatin were acquired at 105,000× magnification in super-resolution mode (pixel size 0.65 Ų) with a dose of 50 e-/Ų (dose-fractionated) and a defocus of ‒3 µm.
Manger S., Ermel U.H, & Frangakis A.S. (2021). Ex vivo visualization of RNA polymerase III-specific gene activity with electron microscopy. Communications Biology, 4, 234.
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6

Graphene Oxide Grid Preparation for Cryo-EM

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C‐flat™ (CF‐2/1‐2C) grids were coated with graphene oxide as previously described (Martin et al, 2016). 3.5 μl of the sample at 0.2 mg/ml was loaded on the copper side and then blotted on the same side for 2 s in a Leica EM GP at 80% humidity and 4°C, before being plunge‐frozen in liquid ethane (−184°C). Micrographs (Appendix Fig S2B) at a nominal magnification of 120,000× were collected in a Talos Arctica electron microscope equipped with a Falcon 3EC camera (Thermo Fisher, Waltham, MA, USA) in linear mode and with a pixel size of 1.24 Å. Dose‐fractionated movie frames 20/micrograph were acquired for 1 s with a total electron flux of 120 e/Å/s. The defocus range chosen for the automatic collect was 0.7 to 2 μm, which resulted in an actual range between 0.4 and 5 μm.
For the amphipole‐containing MC collection, 3019 movies composed of 25 frames at a defocus range between 0.7 and 2 μm were collected at 1.38 Å pixel size with a 5 s exposure time and 15 e/pix/s exposure rate at the Krios 2 at the Diamond eBIC facility.
Rapisarda C., Cherrak Y., Kooger R., Schmidt V., Pellarin R., Logger L., Cascales E., Pilhofer M., Durand E, & Fronzes R. (2019). In situ and high‐resolution cryo‐EM structure of a bacterial type VI secretion system membrane complex. The EMBO Journal, 38(10), e100886.
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7

Cryo-EM Imaging of HUWE1N Protein

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4 μL of HUWE1N at 0.8 mg/mL were applied to a Quantifoil R2/2 Cu 200 mesh grid, freshly glow-discharged at 20 mA for 60 s in a SCD 005 Sputter Coater (BAL-TEC). After 1 s pre-blotting time, the sample was blotted for 2 s with a relative humidity of 70% and a temperature of 4°C in an EM GP freeze plunger (Leica Microsystems). Cryo-EM grids were screened using a Glacios equipped with a Falcon3EC camera (Thermo Fisher Scientific). The selected grid was recorded on a Titan Krios electron microscope (ThermoFisher) equipped with a K3 camera (Gatan) in counting mode at the Institute of Science and Technology Austria. The dataset was recorded both untilted and at 25° stage tilt. The microscope was operated in nanoprobe mode with a beam diameter of 1200 nm at a nominal magnification of 105 000x, resulting in a calibrated pixel size of 0.86 Å per pixel. Images were collected in super-resolution. Four images were taken per hole from different non-overlapping areas using image beam shift. The total electron dose of 60 electrons per Å2 (link) was fractionated into 40 frames. A total number of 2580 movies were acquired without tilt, and 1958 movies were acquired at tilt. A defocus range from −2 to −3.5 μm was used.
Grabarczyk D.B., Petrova O.A., Deszcz L., Kurzbauer R., Murphy P., Ahel J., Vogel A., Gogova R., Faas V., Kordic D., Schleiffer A., Meinhart A., Imre R., Lehner A., Neuhold J., Bader G., Stolt-Bergner P., Böttcher J., Wolkerstorfer B., Fischer G., Grishkovskaya I., Haselbach D., Kessler D, & Clausen T. (2021). HUWE1 employs a giant substrate-binding ring to feed and regulate its HECT E3 domain. Nature chemical biology, 17(10), 1084-1092.
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