Formvar carbon coated 200 mesh copper grids

Manufactured by Electron Microscopy Sciences

Sourced in Switzerland, Austria, United States

Formvar/carbon-coated 200-mesh copper grids are a type of sample support used in electron microscopy. These grids consist of a copper mesh coated with a thin film of formvar and carbon, providing a stable and conductive support for specimens during examination under an electron microscope.

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16 protocols using formvar carbon coated 200 mesh copper grids

TEM Imaging of Biological Samples

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A 10 μl droplet of the sample was deposited on Formvar/carbon-coated 200-mesh copper grids (Electron Microscopy Sciences). The grids were washed twice with 5 μl of ultrapure water and then stained twice with 5 μl of an aqueous 2% w/v uranyl-formate solution and then vacuum-dried from the edges of the grids. Samples were imaged using a Tecnai Spirit BioTWIN electron microscope (TEM) operated at 80 kV with a LaB₆ source.

Ruggeri F.S., Mahul-Mellier A.L., Kasas S., Lashuel H.A., Longo G, & Dietler G. (2017). Amyloid single-cell cytotoxicity assays by nanomotion detection. Cell Death Discovery, 3, 17053-.

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Negative-Stain TEM Analysis of Bacterial Vesicles

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OMV and SyBV were analyzed by negative-stain TEM. The vesicles were applied onto glow-discharged formvar carbon-coated 200-mesh copper grids (Electron Microscopy Sciences, Hatfield, PA). After washing with water, the vesicles were fixed with 2.5% glutaraldehyde dissolved in PBS, followed by staining with 2% uranyl acetate for 1.5 min. Negative-stained bacterial vesicles were visualized using a LEO 912AB Omega electron microscope (Carl Zeiss SMT, Oberkochen, Germany) at 120 kV with a Veleta CCD camera (Olympus-SiS, Stuttgart, Germany).

Park K.S., Svennerholm K., Crescitelli R., Lässer C., Gribonika I., Andersson M., Boström J., Alalam H., Harandi A.M., Farewell A, & Lötvall J. (2023). Detoxified synthetic bacterial membrane vesicles as a vaccine platform against bacteria and SARS-CoV-2. Journal of Nanobiotechnology, 21, 156.

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Transmission Electron Microscopy of Extracellular Vesicles

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Approximately five mL of each EV suspension was applied for five minutes onto formvar/carbon-coated 200 mesh copper grids (Electron Microscopy Sciences) that were glow-discharged (20 mA for 60 s) right before use. EVs were negatively stained with 1% uranyl acetate (Electron Microscopy Sciences, Hatfield, PA, USA) for one minute and air-dried before imaging. A FEI Talos™ F200X transmission electron microscope operated at 200 kV was used. Images were acquired with a Thermo Scientific™ Ceta 16M CMOS (Waltham, MA, USA) camera at a relative magnification of 58,000× (field of view 883.1 nm, pixel size 215.6 pm, defocus ~1 mm). Thermo Scientific Maps Software version 3.18 was used for the automated acquisition of 20 × 20 tiled images to create a large field of view. Representative images were trimmed from large tiles using Adobe Photoshop, modifying brightness and contrast if necessary.

Hindle J., Williams A., Kim Y., Kim D., Patil K., Khatkar P., Osgood Q., Nelson C., Routenberg D.A., Howard M., Liotta L.A., Kashanchi F, & Branscome H. (2024). hTERT-Immortalized Mesenchymal Stem Cell-Derived Extracellular Vesicles: Large-Scale Manufacturing, Cargo Profiling, and Functional Effects in Retinal Epithelial Cells. Cells, 13(10), 861.

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Lignin Particle Size Characterization

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The particle size
of lignin was characterized
by both dynamic light scattering (DLS) and transmission electron microscopy
(TEM). Native lignin, OL, and UL solutions (2% w/v) were prepared
to measure their volume distribution and volume-mean diameters by
DLS (HORIBA Laser Scattering Particle Size Distribution Analyzer LA-910).
A Philips CM 100 (FEI Company, Hillsboro, OR) transmission electron
microscope was used to study the microstructure of native lignin,
OL, and UL. All samples were diluted to 0.2% with deionized (DI) water
and absorbed onto Formvar/carbon-coated 200-mesh copper grids (Electron
Microscopy Sciences, Fort Washington, PA). The morphological properties
of each sample were recorded with the transmission electron microscope
operating at an accelerating voltage of 100 kV.

Zhu X., Wang D., Li N, & Sun X.S. (2017). Bio-Based Wood Adhesive from Camelina Protein (a Biodiesel Residue) and Depolymerized Lignin with Improved Water Resistance. ACS Omega, 2(11), 7996-8004.

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Visualizing Tau Fibril Structures

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Formvar/carbon-coated 200 mesh copper grids (Electron Microscopy Sciences) were covered for 1.5 min with 10-μl droplets of diluted tau fibrils (∼2.5 μM), blotted on filter paper to remove excess liquid, covered for 1.5 min with droplets of 2% uranyl acetate (Electron Microscopy Sciences; 0.2 μm syringe filtered), and again blotted on filter paper. The grids were air dried and then stored until use. Images were recorded with an FEI Tecnai T12 Biotwin electron microscope at 100 KeV equipped with a Gatan CCD camera. Fibril lengths were quantified using ImageJ software.

Weismiller H.A., Holub T.J., Krzesinski B.J, & Margittai M. (2021). A thiol-based intramolecular redox switch in four-repeat tau controls fibril assembly and disassembly. The Journal of Biological Chemistry, 297(3), 101021.

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Exosome Size Characterization by TEM

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Isolated exosomes were resuspended in 0.1 M sodium cacodylate buffer pH 7.2 to a required concentration, and 5μl was placed onto formvar carbon coated 200 mesh copper grids (Electron Microscopy Sciences, Hatfield, PA) for 1 min and removed. The grids were then fixed with 4% glutaraldehyde in sodium cacodylate buffer for 5 min and washed. They were stained with 2% aqueous uranyl acetate for 1 min, and imaged with a FEI Talos F200X Transmission Electron Microscope (Brno, Czech Republic) at 80 KV. The size of exosomes was ascertained from electron microscopy images using Image J software and calibrated magnification bars on the images.

Mukhamedova N., Hoang A., Dragoljevic D., Dubrovsky L., Pushkarsky T., Low H., Ditiatkovski M., Fu Y., Ohkawa R., Meikle P.J., Horvath A., Brichacek B., Miller Y.I., Murphy A., Bukrinsky M, & Sviridov D. (2019). Exosomes containing HIV protein Nef reorganize lipid rafts potentiating inflammatory response in bystander cells. PLoS Pathogens, 15(7), e1007907.

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Ultrastructural Analysis of aSyn Fibrils

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To examine the ultrastructure of aSyn fibrils, negative staining electron microscope images were taken using Formvar/carbon-coated 200-mesh copper grids (Electron microscopy Sciences, Switzerland) as previously described^{94 (link)}. Activated grids were loaded with 5 µl of sample for 30 s, washed three times with ultrapure water, and then negatively stained with 1% uranyl acetate for 1 min. Excess liquid was removed, and grids were allowed to air dry. Imaging was carried out on a Tecnai Spirit BioTWIN electron microscope operating at 80 kV acceleration voltage and equipped with a digital camera (FEI Eagle, FEI). A total of 3–5 images for each sample were chosen and the length of fibrils quantified (average 50–100 nm) using the Image J software (U.S. National Institutes of Health, MD, USA; RRID:SCR_001935).

Lashuel H.A., Mahul-Mellier A.L., Novello S., Hegde R.N., Jasiqi Y., Altay M.F., Donzelli S., DeGuire S.M., Burai R., Magalhães P., Chiki A., Ricci J., Boussouf M., Sadek A., Stoops E., Iseli C, & Guex N. (2022). Revisiting the specificity and ability of phospho-S129 antibodies to capture alpha-synuclein biochemical and pathological diversity. NPJ Parkinson's Disease, 8, 136.

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Negative Staining for Electron Microscopy

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The samples (3.5 μl) were applied onto glow-discharged Formvar/carbon-coated 200-mesh copper grids (Electron Microscopy Sciences) for 1 min. The grids were blotted with filter paper, washed twice with ultrapure water and once with staining solution (uranyl formate 0.7% (w/V)), and then stained with uranyl formate for 30 s. The grids were blotted and dried.

Ait-Bouziad N., Lv G., Mahul-Mellier A.L., Xiao S., Zorludemir G., Eliezer D., Walz T, & Lashuel H.A. (2017). Discovery and characterization of stable and toxic Tau/phospholipid oligomeric complexes. Nature Communications, 8, 1678.

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Transmission Electron Microscopy Sample Prep

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Samples were deposited on Formvar/carbon-coated 200-mesh copper grids (Electron Microscopy Sciences) for 1 min at room temperature, and then grids were washed and stained with 0.75% (w/v) uranyl formate (Electron Microscopy Sciences) solution in water. Prepared grids were imaged using a Tecnai Spirit BioTWIN microscope at 80 kV (LaB6 gun, 0.34 nm line resolution) equipped with a 4k × 4k Eagle CCD camera with a high-sensitivity scintillator from FEI.

DeGuire S.M., Ruggeri F.S., Fares M.B., Chiki A., Cendrowska U., Dietler G, & Lashuel H.A. (2018). N-terminal Huntingtin (Htt) phosphorylation is a molecular switch regulating Htt aggregation, helical conformation, internalization, and nuclear targeting. The Journal of Biological Chemistry, 293(48), 18540-18558.

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Ultrastructural Analysis of BSA-Gold Endocytosis

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After the uptake of BSA-gold (Cell Microscopy Core, Universitair Medisch Centrum Utrecht, Netherlands), HUVECs were fixed at room temperature for 2 h in 2.5% glutaraldehyde in PHEM buffer, pH 7.2 (60 mM 1,4 piperazine diethylsulfonic acid (PIPES), 25 mM 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES), 10 mM EGTA, 2 mM MgCl₂, pH 7.2). After washes with PHEM, the cells were postfixed with 1% osmium and 1.5% potassium ferricyanide (Merck, Darmstadt, Germany) in PHEM before dehydration with a graded series of ethanol and infiltration with epoxy resin. The resin was polymerized at 60 °C for 48 h. Sections with a nominal thickness of 70 nm were obtained with a UC7 ultramicrotome (Leica Microsystems, Vienna, Austria) and collected on formvar/carbon-coated 200 mesh copper grids (Electron Microscopy Sciences, Hatfield, PA, USA). Sections were contrasted with 4% uranyl acetate and Reynold’s lead citrate and observed with a Tecnai Spirit (Thermo Fisher, Eindhoven, Netherlands) operated at 120 kV. Images were acquired using a Gatan Ultra Scan™ 4000 digital camera (Gatan, Pleasanton, USA).

Wu Y., Mahtal N., Paillares E., Swistak L., Sagadiev S., Acharya M., Demeret C., Werf S.V., Guivel-Benhassine F., Schwartz O., Petracchini S., Mettouchi A., Caramelle L., Couvineau P., Thai R., Barbe P., Keck M., Brodin P., Machelart A., Sencio V., Trottein F., Sachse M., Chicanne G., Payrastre B., Ville F., Kreis V., Popoff M.R., Johannes L., Cintrat J.C., Barbier J., Gillet D, & Lemichez E. (2022). C910 chemical compound inhibits the traffiking of several bacterial AB toxins with cross-protection against influenza virus. iScience, 25(7), 104537.

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