Cu pd grids

Manufactured by Agar Scientific

Sourced in United Kingdom

Cu/Pd grids are a type of specimen support used in electron microscopy. They provide a stable and conductive substrate for samples to be observed under an electron beam. The grids are typically made of a copper (Cu) mesh coated with a thin layer of palladium (Pd) to enhance conductivity and stability.

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Lab products found in correlation

Morada ccd camera, by Olympus (6 mentions) Mica chips, by Agar Scientific (4 mentions) Morgagni 268d tem, by Thermo Fisher Scientific (3 mentions) Morgagni 268d, by Thermo Fisher Scientific (1 mentions)

Close spelling variants of this product

Formvar/carbon coated Cu‐Pd 200 mesh grids Cu/Pd TEM grids

6 protocols using cu pd grids

Cohesin Complexes Analyzed by EM

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Cohesin was diluted to a concentration of approximately 0.1 mg/mL in FLAG buffer in the absence or presence of 1 μM rapamycin. Hinge domains were diluted to 0.1 mg/ml in 20 mM Tris pH 7.5, 100 mM NaCl. Samples were subsequently diluted 1:1 in spraying buffer, containing 200 mM ammonium acetate and 60% (v/v) glycerol, pH adjusted to 7.6.
After dilution, the samples were sprayed onto freshly cleaved mica chips (Agar Scientific, UK) and immediately transferred into a BAL-TEC MED020 high vacuum evaporator (BAL-TEC, Liechtenstein) equipped with electron guns. While rotating, samples were coated with 0.7 nm Platinum (BALTIC, Germany) at an angle of 4-5°, followed by 8 nm Carbon (Balzers, Liechtenstein) at 90°. The obtained replicas were floated off from the mica chips, picked up on 400 mesh Cu/Pd grids (Agar Scientific, UK), and inspected in an FEI Morgagni 268D TEM (FEI, the Netherlands) operated at 80 kV. Positions on the grid were chosen randomly. Images were acquired using an 11 megapixel Morada CCD camera (Olympus-SIS, Germany).

Bauer B.W., Davidson I.F., Canena D., Wutz G., Tang W., Litos G., Horn S., Hinterdorfer P, & Peters J.M. (2021). Cohesin mediates DNA loop extrusion by a “swing and clamp” mechanism. Cell, 184(21), 5448-5464.e22.

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Cohesin Trimer Preparation and Imaging

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Cohesin trimer was first diluted to a concentration of approximately 0.1 mg mL⁻¹ in 50 mM sodium phosphate buffer pH 7.6 (including 150 mM NaCl, 5% glycerol and 0.5 mM TCEP) and subsequently diluted 1:1 in spraying buffer, containing 200 mM ammonium acetate and 60% (v/v) glycerol, pH adjusted to 7.6. After dilution, the samples were sprayed onto freshly cleaved mica chips (Agar Scientific, UK) and immediately transferred into a BAL-TEC MED020 high vacuum evaporator (BAL-TEC, Liechtenstein) equipped with electron guns. While rotating, samples were coated with 0.7 nm Platinum (BALTIC, Germany) at an angle of 4-5°, followed by 7 nm Carbon (Balzers, Liechtenstein) at 90°. The obtained replicas were floated off from the mica chips, picked up on 400 mesh Cu/Pd grids (Agar Scientific, UK), and inspected in an FEI Morgagni 268D TEM (FEI, The Netherlands) operated at 80 kV. Images were acquired using an 11 megapixel Morada CCD camera (Olympus-SIS, Germany).

Sonn-Segev A., Belacic K., Bodrug T., Young G., VanderLinden R.T., Schulman B.A., Schimpf J., Friedrich T., Dip P.V., Schwartz T.U., Bauer B., Peters J.M., Struwe W.B., Benesch J.L., Brown N.G., Haselbach D, & Kukura P. (2020). Quantifying the heterogeneity of macromolecular machines by mass photometry. Nature Communications, 11, 1772.

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Ultrastructural Analysis of Arabidopsis Seedlings

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Ten-day old seedlings exposed 7 days to 0.7 mM DEX were fixed using 2% glutaraldehyde and 2% paraformaldehyde in 0.1 M Sodium Cacodylate Buffer (NaCB). Seedlings were kept in a desiccator for 2 h and o/n rotation at room temperature. Washings were performed with 0.1 M NaCB, followed by subsequent steps: staining with 1% Osmium tetroxide in 0.1 M NaCB on ice for 40 min, two rinsing steps in NaCB, one rinsing step in ddH₂O. Samples were dehydrated in a graded series of acetone (40, 60, 80 and 100%) on ice, and embedded in Agar 100 epoxy resin. Seventy nm sections were collected with 100 mesh Cu/Pd grids (Agar Scientific) and post-stained with 2% uranyl acetate and Reynolds lead citrate. Sections were examined with an FEI Morgagni 268D (FEI, Eindhoven, The Netherlands) at 80 kV. Images were acquired using an 11 megapixel Morada CCD camera (Olympus-SIS).

Talloji P., Nehlin L., Hüttel B., Winter N., Černý M., Dufková H., Hamali B., Hanczaryk K., Novák J., Hermanns M., Drexler N., Eifler K., Schlaich N., Brzobohatý B, & Bachmair A. (2022). Transcriptome, metabolome and suppressor analysis reveal an essential role for the ubiquitin-proteasome system in seedling chloroplast development. BMC Plant Biology, 22, 183.

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Negative Stain TEM Imaging of TbMORN1 Proteins

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TbMORN1 and TbMORN1(2–15) were purified according to the two-step procedure detailed above. They were then diluted in spraying buffer (100 mM NH₄CH₃CO₂-NaOH pH 8.5, 30% (v/v) glycerol) to a final concentration of 50–100 μg/ml. Diluted samples were sprayed onto freshly cleaved mica chips (Christine Gröpl) and immediately transferred into a MED020 high vacuum evaporator (BAL-TEC) equipped with electron guns. While rotating, samples were coated with 0.6 nm of Platinum (BALTIC) at an angle of 4°, followed by 6 nm of Carbon (Oerlicon) at 90°. The obtained replicas were floated off the mica chips, transferred to 400 mesh Cu/Pd grids (Agar Scientific), and examined using a Morgagni 268D transmission electron microscope (FEI) operated at 80 kV. Images were acquired using an 11 megapixel Morada CCD camera (Olympus-SIS).

Sajko S., Grishkovskaya I., Kostan J., Graewert M., Setiawan K., Trübestein L., Niedermüller K., Gehin C., Sponga A., Puchinger M., Gavin A.C., Leonard T.A., Svergun D.I., Smith T.K., Morriswood B, & Djinovic-Carugo K. (2020). Structures of three MORN repeat proteins and a re-evaluation of the proposed lipid-binding properties of MORN repeats. PLoS ONE, 15(12), e0242677.

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Platinum-carbon coating for RNA imaging

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Ex-virion RNA in 100 mM Na⁺ or K⁺ phosphate buffer (pH 7.4) was prepared as detailed in Section 2.4. The RNA samples were first diluted to ~0.1 mg/mL in the absence (control) or presence of 20 µM PDS and incubated for 10 min at ambient temperature. The samples were subsequently diluted 1:1 in spraying buffer (200 mM ammonium acetate and 60% (v/v) glycerol, pH adjusted to 7.4). Samples were immediately sprayed onto freshly cleaved mica chips (Agar Scientific, Birchanger, Essex, UK) and quickly transferred into a BAL-TEC MED020 high vacuum evaporator equipped with electron guns. While rotating, samples were coated with 0.6 nm platinum (BALTIC) at an angle of 7°, followed by 6 nm carbon (Balzers, Liechtenstein) at 90°. The replicas were floated off the mica chips, picked up on 400-mesh Cu/Pd grids (Agar Scientific), and inspected in an FEI Morgagni 268D TEM (Thermo Fisher Scientific) operated at 80 kV. Images were acquired using an 11-megapixel Morada CCD camera (Olympus SIS, Münster, Germany).

Real-Hohn A., Groznica M., Kontaxis G., Zhu R., Chaves O.A., Vazquez L., Hinterdorfer P., Kowalski H, & Blaas D. (2023). Stabilization of the Quadruplex-Forming G-Rich Sequences in the Rhinovirus Genome Inhibits Uncoating—Role of Na+ and K+. Viruses, 15(4), 1003.

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Protein Sample Preparation for TEM Imaging

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Purified protein samples were first diluted to a concentration of approximately 0.1 mg/ml using a buffer containing 20 mM Tris pH 7.5, 150 mM NaCl, 1 mM DTT, and subsequently diluted in a 1:1 ratio in the spraying buffer containing 200 mM ammonium acetate and 60% (v/v) glycerol, pH 7.6. After dilution, the samples were sprayed onto freshly cleaved mica chips (Agar Scientific, UK) and immediately transferred into a BAL-TEC MED020 high vacuum evaporator (BAL-TEC, Liechtenstein) equipped with electron guns. While rotating, samples were coated with a 0.7-nm-thick layer of platinum (BALTIC, Germany) at an angle of 4–5°, followed by a 6–7 nm layer of carbon (Balzers, Liechtenstein) at 90°. The replicas obtained were floated off from the mica chips, picked up on 400 mesh Cu/Pd grids (Agar Scientific, UK), and observed in an FEI Morgagni 268D TEM (FEI, The Netherlands) operated at 80 kV. Images were acquired using an 11 megapixel Morada CCD camera (Olympus-SIS, Germany).

Fatalska A., Stepinac E., Richter M., Kovacs L., Pietras Z., Puchinger M., Dong G., Dadlez M, & Glover D.M. (2021). The dimeric Golgi protein Gorab binds to Sas6 as a monomer to mediate centriole duplication. eLife, 10, e57241.

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