Eagle 4k x 4k ccd camera

Manufactured by Thermo Fisher Scientific

The Eagle 4k x 4k CCD camera is a high-resolution imaging device designed for scientific and industrial applications. It features a 4096 x 4096 pixel sensor with a pixel size of 9 microns, providing a large field of view and high image quality. The camera supports various readout modes, exposure times, and binning options to optimize performance for different imaging requirements.

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Eagle 4k × 4k CCD camera (47 citations) Eagle CCD camera (46 citations) Eagle 4k CCD camera (29 citations) Eagle 4k × 4k camera (18 citations) CCD camera (18 citations) 4K × 4K CCD camera (12 citations) 4k Eagle Camera (10 citations) Eagle 4k CCD (5 citations) Eagle 4K x 4K (3 citations) Eagle 4k × 4k (2 citations)

25 protocols using eagle 4k x 4k ccd camera

Cryo-EM Structural Analysis of SARS-CoV-2 Fab Complex

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A three-fold molar excess of Fab was incubated with SARS-2 CoV 6P Mut7 for 30 minutes at room temperature and deposited on a glow discharged carbon coated Cu grid. The complexes were stained with 2% uranyl formate (w/v) for 90 seconds. An FEI Tecnai Spirit at 120 keV paired with an FEI Eagle 4k x 4k CCD camera was used for data collection, and automated using the Leginon software [44 (link)]. Raw micrographs were stored in the Appion database [45 (link)]. Particles were picked with DogPicker [46 (link)] and data was processed in RELION 3.0 [47 (link)]. Figs were generated using UCSF Chimera [48 (link)].

Hingankar N., Deshpande S., Das P., Rizvi Z.A., Wibmer C.K., Mashilo P., Ansari M.Y., Burns A., Barman S., Zhao F., Mukherjee S., Torres J.L., Chattopadhyay S., Mehdi F., Sutar J., Rathore D.K., Pargai K., Singh J., Sonar S., Jakhar K., Dandotiya J., Bhattacharyya S., Mani S., Samal S., Singh S., Kshetrapal P., Thiruvengadam R., Batra G., Medigeshi G., Ward A.B., Bhatnagar S., Awasthi A., Sok D, & Bhattacharya J. (2022). A combination of potently neutralizing monoclonal antibodies isolated from an Indian convalescent donor protects against the SARS-CoV-2 Delta variant. PLoS Pathogens, 18(4), e1010465.

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SARS-CoV-2 Spike Protein Structural Characterization

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The bispecific antibodies were incubated with SARS-2 CoV 6P Mut7 at equal molar ratios for 30 minutes at room temperature. The complexes were diluted to 0.03 mg/ml in 1X TBS pH 7.4 and applied to plasma-cleaned (Argon/Oxygen mix) copper mesh grids. Uranyl formate at 2% was applied to the grid for 55 seconds and then blotted off. Datasets were collected with a FEI Tecnai Spirit (120KeV, 56,000x magnification) paired with a FEI Eagle (4k x 4k) CCD camera. Data collection details include a defocus value −1.5 μm, a pixel size of 2.06 Å per pixel, and a dose of 25 e⁻/Å². Data collection automation was achieved with the Leginon (69 (link)) software and resulting images were stored in the Appion (70 (link)) database. Complexed single particles were picked using DogPicker (71 (link)) and stacked with a box size of 300 pixels. RELION 3.0 (72 (link)) was used for 2D and 3D classifications and final refinements. UCSF Chimera (73 (link)) enabled map segmentation and model docking.

Cho H., Gonzales-Wartz K.K., Huang D., Yuan M., Peterson M., Liang J., Beutler N., Torres J.L., Cong Y., Postnikova E., Bangaru S., Talana C.A., Shi W., Yang E.S., Zhang Y., Leung K., Wang L., Peng L., Skinner J., Li S., Wu N.C., Liu H., Dacon C., Moyer T., Cohen M., Zhao M., Lee F.E., Weinberg R.S., Douagi I., Gross R., Schmaljohn C., Pegu A., Mascola J.R., Holbrook M., Nemazee D., Rogers T.F., Ward A.B., Wilson I.A., Crompton P.D, & Tan J. (2021). Bispecific antibodies targeting distinct regions of the spike protein potently neutralize SARS-CoV-2 variants of concern. Science Translational Medicine, 13(616), eabj5413.

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Cryo-EM Structural Analysis of Protein Complexes

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Purified complexes were diluted to 0.03 mg/ml using 1X TBS pH 7.4, deposited on glow-discharged carbon coated copper mesh grids, and stained for 90 sec with 2% uranyl formate (w/v). Samples were imaged either on a FEI Tecnai Spirit T12 transmission electron microscope (120 keV, 52,000x mag, 2.06 Å per pixel, -1.5 μm defocus) equipped with an FEI Eagle 4k x 4k CCD camera or a FEI TF20 transmission electron microscope (200 keV, 62,000x mag, 1.78 Å per pixel, -1.5 μm defocus) equipped with a TVIPS TemCam F416 CMOS 4k x 4k camera. Collection of raw micrographs was automated with the Leginon (Suloway et al., 2005 (link)) software and stored in the Appion (Lander et al., 2009 (link)) database. For each mouse group complex, enough micrographs were collected to have ≥ 100k particles for data processing. Particles were picked using DogPicker (Voss et al., 2009 (link)), and further data processing was performed in RELION 3.0 (Scheres, 2012 (link)). For EMPEM with SARS-CoV-2 spike, an initial model was generated from a published SARS-CoV-2 S protein structure (PDB: 6VYB (Walls et al., 2020 (link))) and used during data processing. Map interpretation and segmentation was performed in UCSF Chimera (Pettersen et al., 2004 (link)).

Tas J.M., Koo J.H., Lin Y.C., Xie Z., Steichen J.M., Jackson A.M., Hauser B.M., Wang X., Cottrell C.A., Torres J.L., Warner J.E., Kirsch K.H., Weldon S.R., Groschel B., Nogal B., Ozorowski G., Bangaru S., Phelps N., Adachi Y., Eskandarzadeh S., Kubitz M., Burton D.R., Lingwood D., Schmidt A.G., Nair U., Ward A.B., Schief W.R, & Batista F.D. (2022). Antibodies from primary humoral responses modulate the recruitment of naive B cells during secondary responses. Immunity, 55(10), 1856-1871.e6.

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Negative Stain Electron Microscopy

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EM experiments were performed [29 ] using an FEI Tecnai T12 electron microscope, operating at 120 keV equipped with an FEI Eagle 4k x 4k CCD camera. Negative stain grids were transferred into the electron microscope using a room temperature stage. Images of each grid were acquired at multiple scales to assess the overall distribution of the specimen. After identifying potentially suitable target areas for imaging at lower magnifications, high magnification images were acquired at nominal magnifications of 110,000X (0.10 nm/pixel) or 67,000X (0.16 nm/pixel). The images were acquired at a nominal underfocus of -2 μm (110,000X) or -3 μm to -2 μm (67,000X), and electron doses of ~25–40 e/Å².

Chen Q., Vieth M., Timm D.E., Humblet C., Schneidman-Duhovny D., Chemmama I.E., Sali A., Zeng W., Lu J, & Liu L. (2017). Reconstruction of 3D structures of MET antibodies from electron microscopy 2D class averages. PLoS ONE, 12(4), e0175758.

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Cryo-TEM Imaging of Nanoparticles

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The Cryo-TEM was conducted following our previously described protocol^{35 (link)}. Briefly, a 3 µL sample of NP in PBS was dispensed onto a glow discharged copper grid (300 mesh) with lacey carbon film coating (ProSciTech, QLD, Australia). The grid was blotted against filter paper (Whatman 541) and plunged into liquid ethane using an in-house plunge freezing device in 80% humidity. The samples were presented to the transmission electron microscope TEM (FEI, Eindhoven, The Netherlands) operated at 120 kV using a Gatan 626 cryo-holder (Gatan, Pleasanton, CA, USA). A low electron dose of 8–10 electrons/Å² was employed. Images were captured using a FEI Eagle 4kx4k CCD camera (FEI) and AnalySIS software v3.2 (Olympus.).

Sheykhzadeh S., Luo M., Peng B., White J., Abdalla Y., Tang T., Mäkilä E., Voelcker N.H, & Tong W.Y. (2020). Transferrin-targeted porous silicon nanoparticles reduce glioblastoma cell migration across tight extracellular space. Scientific Reports, 10, 2320.

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Transmission Electron Microscopy of Purified Samples

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10-μl drops of purified samples were adsorbed onto freshly glow-discharged 400 mesh carbon-coated copper grids (Electron Microscopy Sciences) for 1 minute and washed in 1–3 drops of (50 μl) 0.1 M and 0.01 M ammonium acetate solutions each. Then, the grids were stained using a freshly filtered 2% solution of uranyl acetate and air-dried after removing the excess stain with filter paper. The stained samples were examined with a Tecnai G20 transmission electron microscope (FEI Company) operating at an acceleration voltage of 200 kV. Electron micrographs were recorded with an Eagle 4k x 4k CCD camera (FEI Company). Defocus levels of 1–2 μm were applied for recording the images. Micrographs acquired for image processing purposes, were recorded at a nominal magnification of 29,000x with a pixel size of 3.07 Å per pixel.

Kamali-Jamil R., Vázquez-Fernández E., Tancowny B., Rathod V., Amidian S., Wang X., Tang X., Fang A., Senatore A., Hornemann S., Dudas S., Aguzzi A., Young H.S, & Wille H. (2021). The ultrastructure of infectious L-type bovine spongiform encephalopathy prions constrains molecular models. PLoS Pathogens, 17(6), e1009628.

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Visualizing Amyloid-beta Aggregates with PLGA

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Aggregates of 10 μM Aβ_1-42 collected from kinetic reaction at different times, native PLGA alone and 10 μM Aβ_1-42 aggregates in the presence or absence of 50 μM PLGA were placed on 200 mesh carbon-coated copper grids for ∼2min followed by a series of washing with ammonium acetate buffer. The washed samples were negatively stained by 2% Na phosphotungstate (pH 7.2) for 10min, washed, dried and then examined using an accelerating voltage of 200 kV. The stained samples were analyzed with a FEI Tecnai G20 TEM and micrographs were recorded using an Eagle 4kx4k CCD camera (FEI Company).

Anand B., Wu Q., Nakhaei-Nejad M., Karthivashan G., Dorosh L., Amidian S., Dahal A., Li X., Stepanova M., Wille H., Giuliani F, & Kar S. (2022). Significance of native PLGA nanoparticles in the treatment of Alzheimer's disease pathology. Bioactive Materials, 17, 506-525.

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Negative Staining of SMALP Samples

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The SMALP sample was diluted in buffer solution (50 mM Sodium phosphate pH 7.0, 100 mM NaCl) to 1 X 10^-5 mg/ml. The sample was then drop cast onto a glow discharged carbon coated electron microscopy grid and negatively stained with Uranyl acetate. Imaging was performed with an FEI Tecnai 12, 120 kV transmission electron microscope (TEM) with an FEI Eagle 4k x 4K CCD camera. All subsequent image processing was carried out using Fiji/ImageJ

Jamshad M., Grimard V., Idini I., Knowles T.J., Dowle M.R., Schofield N., Sridhar P., Lin Y.P., Finka R., Wheatley M., Thomas O.R., Palmer R.E., Overduin M., Govaerts C., Ruysschaert J.M., Edler K.J, & Dafforn T.R. (2014). Structural analysis of a nanoparticle containing a lipid bilayer used for detergent-free extraction of membrane proteins. Nano research, 8(3), 774-789.

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Transmission Electron Microscopy Tissue Preparation

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Tissues were fixed in 2.5% glutaraldehyde and 2% paraformaldehyde in 0.1 M sodium cacodylate buffer pH 7.4 containing 2% sucrose for 1 h and post fixed in 1% osmium tetroxide for 1 h. The sample was rinsed in buffer and en-bloc stained in aqueous 2% uranyl acetate for 1 h followed by rinsing in distilled water, dehydrated in an ethanol series, and infiltrated with Embed 812 (Electron Microscopy Sciences) resin. The samples were placed in silicone molds and baked at 60 °C for 24 h. Hardened blocked were sectioned using a Leica UltraCut UC7. Sixty-nanometer sections were collected on formvar-coated nickel grids and 250-nm sections on copper slot grids and stained using 2% uranyl acetate and lead citrate. Sixty-nanometer sections on grids were viewed FEI Tencai Biotwin TEM at 80 kV. Images were taken using Morada CCD and iTEM (Olympus) cellSens Dimension software.
For electron tomography, 250-nm-thick sections with 15 nm fiducial gold to aid alignment for tomography was done using FEI Tecnai TF20 at 200 kV. Data were collected using SerialEM (Boulder) on a FEI Eagle 4Kx4K CCD camera using tilt angles −60° to 60° and reconstructed using Imod4.9 (University of Colorado Boulder).

Zhou H.J., Qin L., Jiang Q., Murray K.N., Zhang H., Li B., Lin Q., Graham M., Liu X., Grutzendler J, & Min W. (2021). Caveolae-mediated Tie2 signaling contributes to CCM pathogenesis in a brain endothelial cell-specific Pdcd10-deficient mouse model. Nature Communications, 12, 504.

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Cryo-TEM Imaging of Protein Samples

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Cryo-TEM imaging was performed by NanoImaging Services (San Diego, CA). Following reconstitution, each sample was prepared by applying a 3-μL drop of sample to a clean holey carbon film on a 400-mesh copper grid, blotting away with filter paper, and vitrifying in liquid ethane. Prepared grids were stored in liquid nitrogen until transferred to a Tecnai T12 transmission electron microscope (FEI, Hillsboro, OR) operating at 120 keV and equipped with an Eagle 4k x 4k CCD camera (FEI). A cryostage maintained the prepared grids at ≤ -170 °C. Images were collected at 21,000–110,000× magnification at a nominal underfocus of −5 to −2 μm and electron doses of ∼10–20 e⁻/Å².

Archer M.C., McCollum J., Press C., Dutill T.S., Liang H., Fedor D., Kapilow-Cohen L., Gerhardt A., Phan T., Trappler E.H., Orr M.T., Kramer R.M, & Fox C.B. (2023). Stressed stability and protective efficacy of lead lyophilized formulations of ID93+GLA-SE tuberculosis vaccine. Heliyon, 9(6), e17325.

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