Falcon 3 detector

Manufactured by Thermo Fisher Scientific

Sourced in United States, Taiwan, Province of China

The Falcon III detector is a high-performance scientific instrument designed for advanced imaging applications. It features a large active area, high-sensitivity detection, and low noise characteristics. The Falcon III detector is optimized for a wide range of analytical and research applications requiring precise and reliable data acquisition.

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Falcon III (44 citations) Falcon III direct electron detector (39 citations) Falcon-3 direct detector (5 citations) FEI Falcon 3 direct electron detector (4 citations) Falcon III direct electron detector 30 (2 citations)

30 protocols using falcon 3 detector

Cryo-EM Imaging of Frozen Hydrated Samples

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The frozen, hydrated grids were maintained at near-liquid nitrogen temperatures (−176 to −180 °C) during the imaging. The images were collected on a Talos Arctica cryo-electron microscope (ThermoFisher Scientific, Taipei, Taiwan) operated at 200 keV. For the single-particle analysis, the low-dose condition was~48 e⁻/Å². The images were captured at a magnification of 73,000× with a defocus range of −0.5 to −2.5 μm and recorded with a Falcon III detector (ThermoFisher Scientific, Taipei, Taiwan). For the cryo-electron tomography, a series of images were collected automatically from −60° to +60° at 2° intervals using tomography data collection software version 5.6.0.2368REL (ThermoFisher Scientific, Taipei, Taiwan), with a total dose of ~61 e⁻/Å² and a defocus of −3 μm. The images had a magnification of 57,000× and were recorded with a Falcon III detector (ThermoFisher Scientific, Taipei, Taiwan).

Huang H.J., Tang S.L., Chang Y.C., Wang H.C., Ng T.H., Garmann R.F., Chen Y.W., Huang J.Y., Kumar R., Chang S.H., Wu S.R., Chao C.Y., Matoba K., Kenji I., Gelbart W.M., Ko T.P., Wang H.J., Lo C.F., Chen L.L, & Wang H.C. (2023). Multiple Nucleocapsid Structural Forms of Shrimp White Spot Syndrome Virus Suggests a Novel Viral Morphogenetic Pathway. International Journal of Molecular Sciences, 24(8), 7525.

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Cryo-EM and DLS Characterization of Proteoliposomes

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Aliquots of PLs (2.5 μL, 122 μg-CI mL⁻¹) were applied to glow-discharged (90 s at 20 mA) Quantifoil R 2/2 300 mesh copper grids. The grids were plunge-frozen in liquid ethane using an FEI Vitrobot Mark IV at 4 °C in 100% humidity, with a blotting force of −6 for 6 s. Images were collected using a Talos Arctica cryo-TEM (transmission electron microscope) (Thermo Fisher Scientific). The micrographs were recorded using a Falcon III detector (Thermo Fisher Scientific) at a nominal magnification of 73,000× in the linear mode with the EPU software.
For DLS measurements, the vesicle size distribution of 40 μL of a standard CI−Q₁₀−F₁F₀ PL sample was measured in Brand UV cuvettes using a Zetasizer Nano S (Malvern Instruments Ltd.). Technical triplicates were each measured 20 times. The intensity-weighted distributions were converted into volume-weighted distributions to account for over-estimation of large particles,^{45 (link)} using the Zetasizer Software (ver. 7.13).

Biner O., Fedor J.G., Yin Z, & Hirst J. (2020). Bottom-Up Construction of a Minimal System for Cellular Respiration and Energy Regeneration. ACS synthetic biology, 9(6), 1450-1459.

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Cryo-EM Sample Preparation for Virus-Like Particles

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Cryo-EM grids were prepared by applying purified VLPs to 400-mesh lacey carbon grids with an additional ultra-thin (<3nm) continuous carbon film (Agar Scientific, UK). Grids were glow-discharged for 30 seconds prior to sample application (easiGlow, Ted Pella). BYDV VLPs were applied to the grids once but for other samples, to increase the number of particles that adhere to the carbon, 3 μl of the sample was incubated on the grid for 5 minutes. The majority of the liquid evaporated during the incubation, but at no point was the grid allowed to dry; this was repeated a number of times (Table S1). The final 3 μl was blotted immediately using FEI vitrobot mark IV (ThermoFisher) device. Grids were vitrified by plunging into in liquid nitrogen-cooled liquid ethane, at 90% relative humidity and 4°C. All data were collected on a ThermoFisher Titan Krios (Astbury Biostructure Laboratory, University of Leeds) EM at 300 kV, using a dose of 63.2 e^-/Å² for BYDV and 72 e^-/Å² for PLRV, and a magnification of 75,000x (Table S1). Exposures were recorded using the EPU software on a ThermoFisher Falcon III detector, with an object sampling of 1.065 Å/pixel. Each movie had a total exposure of 1.5 seconds and contained 59 frames. Data collection was set up as described previously (Thompson et al., 2019 (link)), and details for each dataset are shown in Table S1.

Byrne M.J., Steele J.F., Hesketh E.L., Walden M., Thompson R.F., Lomonossoff G.P, & Ranson N.A. (2019). Combining Transient Expression and Cryo-EM to Obtain High-Resolution Structures of Luteovirid Particles. Structure(London, England:1993), 27(12), 1761-1770.e3.

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Cryo-EM Analysis of Recombinant USP24

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The recombinant USP24 used for cryo-EM analysis was purchased from OriGene with a concentration of 0.15 mg/ml (CAT#: TP329472, OriGene, USA), and an aliquot of 4 μl was loaded onto a glow-discharged grid coated with a holey carbon film (300 mesh, R2/1, Quatifoil GmbH, Germany). The vitrification of the grids was carried out using a Vitrobot system (Thermo Fisher Scientific, USA) with a waiting time of 3 s and blotting time of 4.5 s. The cryo-EM micrographs were acquired using a 200 kV Talos Arctica transmission electron microscope equipped with a Falcon III detector (Thermo Fisher Scientific, USA) with a magnification of ×120,000, corresponding to a pixel size of 0.86 Å/pixel. The micrographs were processed with motion correction and CTF estimation using cryoSPARC [28 (link)]. For the single particle reconstitution analysis, 16,213 particles were selected from a total of 57,814 particles picked from 2921 micrographs after three runs of 2D classification. The initial map was refined and polished through two rounds of homogenous refinement and was then visualized using Chimera.

Young M.J., Wang S.A., Chen Y.C., Liu C.Y., Hsu K.C., Tang S.W., Tseng Y.L., Wang Y.C., Lin S.M, & Hung J.J. (2024). USP24-i-101 targeting of USP24 activates autophagy to inhibit drug resistance acquired during cancer therapy. Cell Death and Differentiation, 31(5), 574-591.

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Cryo-EM Data Acquisition with Titan Krios

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Cryo-EM grids were first checked on a Talos transmission electron microscope equipped with a Falcon III detector (Thermo Fisher Scientific) operated in linear mode. The images were recorded at a nominal magnification of 120,000x, corresponding to a pixel size of 0.86 Å/pixel, with a defocus setting of -3.0 μm. Suitable cryo-EM grids were recovered for further data collection on a 300 kV Titan Krios transmission electron microscope hosting a K3 detector (with GIF Bio-Quantum Energy Filters, Gatan) operating in super-resolution mode and using EPU-2.7.0 software (Thermo Fisher Scientific). The raw movie stacks were recorded at a magnification of 105,000×, corresponding to a pixel size of 0.83 Å/pixel (super-resolution 0.415 Å/pixel). The defocus range was set to −1.5 to -2.5 μm and the slit width of energy filters was set to 20 eV. Forty frames of non-gain-normalized tiff stacks were recorded with a dose rate of ~16 e-/Å2 per second and the total exposure time was set to 2.5 s, resulting in an accumulated dose of ~40 e-/Å2 (~1.0 e-/Å2 per frame). The parameters for cryo-EM data acquisition are summarized in Table 1.

Liao C.C., Wang Y.S., Pi W.C., Wang C.H., Wu Y.M., Chen W.Y, & Hsia K.C. (2023). Structural convergence endows nuclear transport receptor Kap114p with a transcriptional repressor function toward TATA-binding protein. Nature Communications, 14, 5518.

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Cryo-EM Sample Preparation and Imaging

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Activity assay master mix was prepared as described above and incubated at 30 °C for 30 min. 10 µl of the master mix was loaded on a C-flat (protochips) CF1.2/1.3-4 C grid (1.2 µm holes) that had been prepared by addition of a continuous carbon support film and glow discharged at 25 mA for 1 min. The grids were blotted for 6 seconds at blot force 10, using an FEI Vitrobot Mark IV in chamber conditions of 4°C and 95% relative humidity. These were screened and initial analysis performed using a JEOL 2200 TEM equipped with a Direct Electron DE20 camera, optimised grids were then imaged on a Thermo-Fisher Titan Krios in the Astbury Biostructure Laboratory using a Falcon III detector in integrating mode operated at 40 frames per second. Data were collected at nominal 75,000 x magnification, giving a sampling frequency of 1.065 Å/pixel. Two-second exposures were collected at a dose rate of 54 e⁻/Å² /second and a defocus range of −1.5 to 2 microns.

Loundras E.A., Streetley J., Herod M.R., Thompson R., Harris M., Bhella D, & Stonehouse N.J. (2022). Higher-order structures of the foot-and-mouth disease virus RNA-dependent RNA polymerase required for genome replication. Communications Biology, 5, 61.

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Cryo-EM Tomography Data Acquisition

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Cryo-EM grids were clipped and loaded into a 200 kV Talos Arctica or a 300 kV Titan Krios transmission electron microscope (TEM; Thermo Fisher Scientific). For data collection on Talos Arctica, cryo-EM tilt images were recorded using a Falcon III detector (Thermo Fisher Scientific) operating in linear mode at a magnification of 28,000× with a pixel size of 3.6 Å/pixel. The imaging defocus was set to around –15 μm. Tomographic tilt images were collected using Tomography-4.10.0 software (Thermo Fisher Scientific) with a tilt range of ±60° in 2° increments (from +20° to –60°, and then from +20° to +60°). For each tilt, a dose of ~2 e⁻/Å² was used, and the total dose was ~120 e⁻/Å² for 61 tilt images. For data collection on Titan Krios, cryo-EM tilt images were recorded with a K3 Summit detector (with GIF Bio-Quantum Energy Filters, Gatan) operating in counting mode at a magnification of 33,000x with a pixel size of 2.75 Å/pixel. The defocus for imaging was set to −6 to −15 μm. Tomographic tilt images were collected using Tomography-5.2.0 software (Thermo Fisher Scientific).

Chen E.H., Wang C.H., Liao Y.T., Chan F.Y., Kanaoka Y., Uchihashi T., Kato K., Lai L., Chang Y.W., Ho M.C, & Chen R.P. (2023). Visualizing the membrane disruption action of antimicrobial peptides by cryo-electron tomography. Nature Communications, 14, 5464.

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Reconstitution of mSA-capped Nucleoprotein Filaments

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Mono-streptavidin (mSA)-capped nucleoprotein filaments were reconstituted in buffer: 25 mM HEPES pH 7.5, 150 mM NaCl, 2 mM DTT, 2 mM ATP, 5 mM CaCl₂ supplemented with the appropriate DNA substrate at 250 nM. mSA was first added to a final concentration of 2.5 μM and incubated for 15 minutes at room temperature. RAD51 was then added to a final concentration of 5 μM and the sample was incubated for further 15 minutes to allow for filament formation. The BRCA2 TR2 peptide was added to a final concentration of 40 μM (eight-fold molar excess over RAD51) and incubated for 5 minutes.
UltrAuFoil R1.2/R1.3 300 grids (Quantifoil) were glow-discharged twice for 1 minute using a PELCO easiGlow system (0.38 mBar, 30 mA, negative polarity). 3 μl of sample was applied to each grid before plunge-freezing in liquid ethane using a Vitrobot Mark IV robot (ThermoFisher Scientific), set to 100% humidity, 4 °C, 2 second blot time and −3 blot force.
All cryoEM experiments were carried out at the cryoEM facility of the University of Cambridge in the Department of Biochemistry. CryoEM data collection parameters are reported in Supplementary Table 2. Grids were screened with a 200 keV Talos Arctica microscope fitted with a Falcon III detector (ThermoFisher Scientific) at ×37,000 magnification and with an applied defocus of −4 μM.

Appleby R., Joudeh L., Cobbett K, & Pellegrini L. (2023). Structural basis for stabilisation of the RAD51 nucleoprotein filament by BRCA2. Nature Communications, 14, 7003.

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Cryo-EM Analysis of FIPV-UU4 S Protein

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Four microliters of purified FIPV-UU4 S protein (0.2 mg/mL) in PBS (Sigma-Aldrich; 79382) was applied onto glow-charged 200-mesh Quantifoil R2/1 holey carbon grids. The grids were blotted for 3 s at 4 °C and 100% humidity, and vitrified using a Vitrobot Mark IV (Thermo Fisher). Cryoelectron data of FIPV-UU4 S protein were collected using a 200-keV Talos Arctica microscope with an exposure time of 2.5 s and pixel size of 0.87 Å, using a Falcon III detector (Thermo Fisher) in a linear mode. In total, 2,436 micrographs were collected with defocus ranging between 1.8 and 2.8 µm and accumulated exposure of 48 e⁻/Å² distributed over 32 frames.

Yang T.J., Chang Y.C., Ko T.P., Draczkowski P., Chien Y.C., Chang Y.C., Wu K.P., Khoo K.H., Chang H.W, & Hsu S.T. (2020). Cryo-EM analysis of a feline coronavirus spike protein reveals a unique structure and camouflaging glycans. Proceedings of the National Academy of Sciences of the United States of America, 117(3), 1438-1446.

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Cryo-EM Imaging of AuNPs-Lipid Hybrids

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On glow-discharged Quantifoil
Cu 300 R2/2 grids were applied 3 μL of AuNPs-DOPC and AuNPs-DPPC
hybrids. The hybrids were plunge frozen in liquid ethane using an
FEI Vitrobot Mark IV (Thermo Fisher Scientific) instrument. Excess
liquid was removed by blotting for 1 s (blot force of 1) using filter
paper under 100% humidity and 10 °C. Cryo-EM data were collected
at the Florence Center for Electron Nanoscopy (FloCEN), University
of Florence, on a Glacios (Thermo Fisher Scientific) instrument at
200 kV equipped with a Falcon III detector operated in the counting
mode. Images were acquired using EPU software with a physical pixel
size of 2.5 Å and a total electron dose of ∼ 50 e^–/Å² per micrograph.

Cardellini J., Caselli L., Lavagna E., Salassi S., Amenitsch H., Calamai M., Montis C., Rossi G, & Berti D. (2022). Membrane Phase Drives the Assembly of Gold Nanoparticles on Biomimetic Lipid Bilayers. The Journal of Physical Chemistry. C, Nanomaterials and Interfaces, 126(9), 4483-4494.

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