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Tecnai t12 electron

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The Tecnai T12 electron microscope is a transmission electron microscope (TEM) designed for high-resolution imaging and analysis of materials at the nanoscale. It is equipped with a LaB6 electron source and operates at an accelerating voltage of 120 kV. The Tecnai T12 provides a magnification range from 25x to 1,000,000x and a spatial resolution of 0.34 nm, enabling detailed visualization and characterization of fine structural features.

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Lab products found in correlation

Superdex 200, by GE Healthcare (2 mentions) Temcam f416, by TVIPS (2 mentions) Eagle 4k x 4k ccd camera, by Thermo Fisher Scientific (1 mentions) Formvar carbon coated copper grid, by Ted Pella (1 mentions) Formvar carbon coated copper grids with 200 mesh, by Electron Microscopy Sciences (1 mentions)

Close spelling variants of this product

Tecnai T12 (202 citations) Tecnai T12 electron microscope (104 citations) Tecnai T12 transmission electron microscope (44 citations) Tecnai T12 BioTwin electron microscope (6 citations) Tecnai Spirit (T12) transmission electron microscope (5 citations) Tecnai Spirit T12 electron microscope (4 citations) Tecnai T12 Transmission Electron Microscope (TEM (3 citations) Tecnai™ T12 cryo-electron microscope (3 citations) Tecnai T12 G2 TWIN transmission electron microscope (2 citations) Tecnai T12 TWIN transmission electron microscope (2 citations)

7 protocols using tecnai t12 electron

1

Structural Characterization of NCP-UV-DDB Complex

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NCPs carrying THF2 at position -1 (-22/-23 from the nucleosome dyad position) and purified human UV-DDB were mixed in a 1:2 molar ratio and purified by gel filtration (Superdex 200; GE Healthcare) in 50 mM HEPES pH 7.4, 50 mM NaCl and 250 μM TCEP (GF buffer). Purified NCPTHF2(-1)-UV-DDB was diluted to ~0.03 mg/ml and applied to glow discharged Quantifoil grids (S7/2+2 nm C, Cu 400 mesh, Quantifoil Micro Tools), blotted, and stained with 2% (w/v) uranyl acetate. Data were collected using a Tecnai T12 electron microscope (Thermo Fischer) operating at 100 kV with a pixel size of 3.08 Å at the specimen level. Images were recorded with a TVIPS TemCam F416 with varying defocus (-0.5 µm to -2.0 μm). All particles (12774) were selected using e2boxer.py38 (link) and processed with SPARX39 (link). After two-dimensional (2D) classification with iterative stable alignment and classification in SPARX, the best 115 2D class averages were used for 3D ab initio model generation with sxviper.py from SPARX.
Matsumoto S., Cavadini S., Bunker R.D., Grand R.S., Potenza A., Rabl J., Yamamoto J., Schenk A.D., Schübeler D., Iwai S., Sugasawa K., Kurumizaka H, & Thomä N.H. (2019). DNA damage detection in nucleosomes involves DNA register shifting. Nature, 571(7763), 79-84.
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2

Structural Characterization of NCP-UV-DDB Complex

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NCPs carrying THF2 at position -1 (-22/-23 from the nucleosome dyad position) and purified human UV-DDB were mixed in a 1:2 molar ratio and purified by gel filtration (Superdex 200; GE Healthcare) in 50 mM HEPES pH 7.4, 50 mM NaCl and 250 μM TCEP (GF buffer). Purified NCPTHF2(-1)-UV-DDB was diluted to ~0.03 mg/ml and applied to glow discharged Quantifoil grids (S7/2+2 nm C, Cu 400 mesh, Quantifoil Micro Tools), blotted, and stained with 2% (w/v) uranyl acetate. Data were collected using a Tecnai T12 electron microscope (Thermo Fischer) operating at 100 kV with a pixel size of 3.08 Å at the specimen level. Images were recorded with a TVIPS TemCam F416 with varying defocus (-0.5 µm to -2.0 μm). All particles (12774) were selected using e2boxer.py38 (link) and processed with SPARX39 (link). After two-dimensional (2D) classification with iterative stable alignment and classification in SPARX, the best 115 2D class averages were used for 3D ab initio model generation with sxviper.py from SPARX.
Matsumoto S., Cavadini S., Bunker R.D., Grand R.S., Potenza A., Rabl J., Yamamoto J., Schenk A.D., Schübeler D., Iwai S., Sugasawa K., Kurumizaka H, & Thomä N.H. (2019). DNA damage detection in nucleosomes involves DNA register shifting. Nature, 571(7763), 79-84.
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3

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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4

Transmission Electron Microscopy Imaging

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Samples were adsorbed onto freshly glow-discharged, 200-mesh formvar/carbon-coated copper grids (Ted Pella), washed with water, and stained with 0.7% (w/v) uranyl formate for 15 to 20 s. TEM images were taken on an FEI Tecnai T12 electron microscope.
El Mammeri N., Dregni A.J., Duan P., Wang H.K, & Hong M. (2022). Microtubule-binding core of the tau protein. Science Advances, 8(29), eabo4459.
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5

Characterization of Ag2S-NP and AION Nanoparticles

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Both Ag2S-NP and AION samples were examined using an FEI Tecnai T12 electron microscope with an acceleration voltage of 120 kV. Formvar carbon-coated copper grids with 200 mesh (Electron Microscopy Sciences, Hatfield, PA) were used to prepare the TEM samples. Briefly, 10 μl of diluted Ag2S-NP or AION samples (5 μl from concentrated stock diluted with 495 μl DI water) were dropped onto the grids and allowed to dry before imaging. The core diameter of AION was measured using ImageJ (National Institutes of Health, Bethesda, MD).
Hsu J.C., Naha P.C., Lau K.C., Chhour P., Hastings R., Moon B.F., Stein J.M., Witschey W.R., McDonald E.S., Maidment A.D, & Cormode D.P. (2018). An all-in-one nanoparticle (AION) contrast agent for breast cancer screening with DEM-CT-MRI-NIRF imaging. Nanoscale, 10(36), 17236-17248.
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6

Virus-like Particle Purification and Characterization

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Virus‐like particles were purified as previously described in VLP collections & functional budding assays. Following ultracentrifugation, VLPs were resuspended in fixative (2.5% glutaraldehyde in 0.1 M cacodylate buffer). Purified VLPs were applied onto glow discharged carbon formvar grids and negatively stained using 4% uranyl acetate. Samples were imaged with a FEI Tecnai T12 electron microscope equipped with a tungsten source and operating at 80 kV. VLP length and diameter measurements were quantified using ImageJ software. For diameter analysis, eight different diameters were measured across random areas on each VLP, and the mean diameter was reported.
Husby M.L., Amiar S., Prugar L.I., David E.A., Plescia C.B., Huie K.E., Brannan J.M., Dye J.M., Pienaar E, & Stahelin R.V. (2022). Phosphatidylserine clustering by the Ebola virus matrix protein is a critical step in viral budding. EMBO Reports, 23(11), e51709.
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7

Negative stain EM analysis of PGT124 Fab-BG505 SOSIP complex

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PGT124 Fab in complex with BG505 SOSIP.664 gp140 produced in HEK 293S cells were analyzed by negative stain EM. A 3 μL aliquot of 10 μg/ml of the complex was applied for 15s onto a glow discharged, carbon coated 400 Cu mesh grid and stained with 2% uranyl formate for 20s. Grids were imaged using a FEI Tecnai T12 electron microscope operating at 120 kV using 52,000 × magnification and electron dose of 25 e−/Å2, resulting in a pixel size of 2.05 Å at the specimen plane. Images were acquired with a Tietz 4k × 4k CCD camera in 5° tilt increments from 0° to 55° at a defocus of 1000 nm using LEGINON (Suloway et al., 2005 (link)).
Garces F., Sok D., Kong L., McBride R., Kim H.J., Saye-Francisco K.F., Julien J.P., Hua Y., Cupo A., Moore J.P., Paulson J.C., Ward A.B., Burton D.R, & Wilson I.A. (2014). Structural evolution of glycan recognition by a family of potent HIV antibodies. Cell, 159(1), 69-79.
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