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Eagle 2k hs ccd camera

Manufactured by Thermo Fisher Scientific
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The Eagle 2k HS CCD camera is a high-sensitivity charge-coupled device (CCD) camera designed for scientific imaging applications. It features a 2048 x 2048 pixel sensor and is capable of capturing images with a high dynamic range and low noise levels.

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Lab products found in correlation

Tecnai spirit biotwin tem, by Thermo Fisher Scientific (2 mentions) Gatan 626 cryo holder, by Ametek (2 mentions) Copper grid, by Ted Pella (1 mentions) 626 cryo holder, by Ametek (1 mentions)

Close spelling variants of this product

Eagle 2k × 2k CCD camera Eagle 2k CCD camera Eagle 2K camera 2k × 2k CCD camera Eagle CCD camera CCD camera

5 protocols using eagle 2k hs ccd camera

1

Structural Analysis of BRCA1-BARD1 Complexes

Cited 2 times
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Samples of isolated wild-type, mutated, and modified BRCA1-BARD1 assemblies [0.02 mg/ml in 20 mM Hepes buffer (pH 7.2), 150 mM NaCl, 10 mM CaCl2, 10 mM MgCl2] were applied to glow-discharged, continuous carbon support films on copper grids (Ted Pella) or to EM affinity grids (24 (link), 38 (link)). Affinity grids were decorated with antibodies against the BRCA1 RING domain (EMD Millipore; MS110, AB1) or the BRCT domain (C-20) for labeling studies conducted on wild-type assemblies. Protein complexes were tethered to the antibody-decorated grids by incubating Ni-NTA eluates for 2 min, followed by standard negative staining procedures using 1% uranyl formate (39 (link)). Specimens were examined using a FEI TEM (FEI Company) equipped with a LaB6 filament and operating at 120 kV under low-dose conditions (<5 electrons/Å2). Images were recorded using an Eagle 2k HS CCD camera (FEI Company) with a pixel size of 30 μm at a magnification of about ×68,000 for a final sampling of 4.4 Å/pixel.
Liang Y., Dearnaley W.J., Varano A.C., Winton C.E., Gilmore B.L., Alden N.A., Sheng Z, & Kelly D.F. (2017). Structural analysis of BRCA1 reveals modification hotspot. Science Advances, 3(9), e1701386.
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2

Structural Analysis of Protein Aggregates

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All specimens were examined using an FEI Spirit BioTwin TEM (FEI Company, Hillsboro, OR, USA) equipped with a LaB6 filament operating at 120 kV under low-dose conditions (0.1–1 electron per Å2). Images were recorded using an FEI Eagle 2k HS CCD camera having a pixel size of 30 µm. For real-time acquisition, sequential images were collected at 1 s intervals for a cumulative dose of ~6–8 electron per Å2 for the 30 and 40 s recordings. The image sequences were colored for visualization purposes and contour maps were computed and segmented according to statistical significance in electron density. Image sequences were imported into the iMovie 10.0.7 software package (Apple, Inc.) and the movies were compiled and exported (.mov format) for real-time observation. During data collection, we obtained multiple images for each stressed and unstressed condition and performed each experiment in duplicate. For the liquid cell imaging results, multiple images were collected and movies were produced from these imaging session. Velocity measurements were calculated for protein aggregates occurring in the movie frames using MATLAB.
DiMemmo L.M., Varano A.C., Haulenbeek J., Liang Y., Patel K., Dukes M.J., Zheng S., Hubert M., Piccoli S.P, & Kelly D.F. (2017). Real-time observation of protein aggregates in pharmaceutical formulations using liquid cell electron microscopy. Lab on a chip, 17(2), 315-322.
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3

Cryo-TEM Imaging of Viral Capsids

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Frozen-hydrated specimens were transferred to a 626 Cryo holder (Gatan, Inc.) and maintained in liquid nitrogen until transferred to the TEM. DLPs were imaged using FEI Tecnai Spirit Biotwin TEM (FEI Co.) equipped with a LaB6 filament and operated at acceleration voltage of 120 kV under low-dose conditions (~5 electrons / Å2). Images of inactive and transcriptionally-active DLPs were recorded on a FEI Eagle 2 k HS CCD camera with a pixel size of 30-μm. Defocus values of the images ranged from −1 to −3.0 μm and images were recorded at a nominal magnification of 68,000×, for a final sampling of ~4.4 Å/pixel at the specimen level.
Hauser M., Dearnaley W.J., Varano A.C., Casasanta M., McDonald S.M, & Kelly D.F. (2019). Cryo-EM Reveals Architectural Diversity in Active Rotavirus Particles. Computational and Structural Biotechnology Journal, 17, 1178-1183.
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4

Cryo-TEM Imaging of Transcriptionally-Active DLPs

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Frozen-hydrated specimens were transferred to a Gatan 626 cryo holder (Gatan, Inc.) and maintained under liquid nitrogen until transferred into the TEM. Specimens were imaged using a FEI Tecnai Spirit BioTwin TEM (FEI, Co, Hillsboro, OR) equipped with a LaB6 filament and operated at an acceleration voltage of 120 kV under low-dose conditions (∼5 electrons/ Å2). Images of transcriptionally-active DLPs were recorded on a FEI Eagle 2k HS CCD camera with a pixel size of 30 μm using a defocus range from -1.0 μm to -3.0 μm at a nominal magnification of 60,000× for a final sampling of 5 Å/pixel at the specimen level.
Rahimi A., Varano A.C., Demmert A.C., Melanson L.A., McDonald S.M, & Kelly D.F. (2015). A Non-Symmetric Reconstruction Technique for Transcriptionally-Active Viral Assemblies. Journal of analytical & molecular techniques, 2(1), http://www.avensonline.org/wp-content/uploads/JAMT-2474-1914-02-0004.pdf.
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5

Cryo-TEM Imaging of Transcriptionally-Active DLPs

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Frozen-hydrated specimens were transferred to a Gatan 626 cryo holder (Gatan, Inc.) and maintained under liquid nitrogen until transferred into the TEM. Specimens were imaged using a FEI Tecnai Spirit BioTwin TEM (FEI, Co, Hillsboro, OR) equipped with a LaB6 filament and operated at an acceleration voltage of 120 kV under low-dose conditions (∼5 electrons/ Å2). Images of transcriptionally-active DLPs were recorded on a FEI Eagle 2k HS CCD camera with a pixel size of 30 μm using a defocus range from -1.0 μm to -3.0 μm at a nominal magnification of 60,000× for a final sampling of 5 Å/pixel at the specimen level.
Rahimi A., Varano A.C., Demmert A.C., Melanson L.A., McDonald S.M, & Kelly D.F. (2015). A Non-Symmetric Reconstruction Technique for Transcriptionally-Active Viral Assemblies. Journal of analytical & molecular techniques, 2(1), http://www.avensonline.org/wp-content/uploads/JAMT-2474-1914-02-0004.pdf.
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