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200 mesh carbon coated copper grid

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The 200-mesh carbon-coated copper grid is a laboratory equipment used for transmission electron microscopy (TEM) sample preparation. It consists of a copper mesh grid with a thin carbon coating, providing a stable and conductive surface for mounting and analyzing samples at the nanoscale.

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Lab products found in correlation

Tecnai spirit bio twin transmission electron microscope, by Thermo Fisher Scientific (2 mentions) Uranyl acetate, by Spectrum Chemical (2 mentions) Titan themis 200, by Thermo Fisher Scientific (1 mentions) Ht7700, by Hitachi (1 mentions) Methylamine tungstate, by Ted Pella (1 mentions) H 7500, by Hitachi (1 mentions) Cary 60 uv vis spectrophotometer, by Agilent Technologies (1 mentions) Miseq system, by Illumina (1 mentions) Cm200, by Philips (1 mentions)

10 protocols using 200 mesh carbon coated copper grid

1

Visualization of Peptide Assemblies

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Grids were prepared using diluted aqueous solutions of peptide assemblies in which aliquots of sample (4 μL) were deposited onto a 200-mesh carbon-coated copper grid from Electron Microscopy Services. After 90 s of incubation on the grid, moisture was wicked away, leaving a thin film of sample. An aliquot (4 μL) of negative stain solution, either 1% uranyl acetate for PSMα3 or a 1:1 mixture of 1% methylamine tungstate (nano-W) and 1% methylamine vanadate (nanoVan) stains from Nanoprobes, Inc. for PSMβ2, was deposited onto the thin film. After 60 s of staining, the remaining moisture was wicked away, and the grid was dried in a tabletop desiccator in vacuo for at least 5 min. Electron micrographs were recorded on a Hitachi HT-7700 TEM with a tungsten filament and AMT CCD camera at an accelerating voltage of 80 kV.
Kreutzberger M.A., Wang S., Beltran L.C., Tuachi A., Zuo X., Egelman E.H, & Conticello V.P. (2022). Phenol-soluble modulins PSMα3 and PSMβ2 form nanotubes that are cross-α amyloids. Proceedings of the National Academy of Sciences of the United States of America, 119(20), e2121586119.
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2

Peptide Preparation for TEM Imaging

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TEM Grids were prepared using dilute solutions of peptide (3 mg/mL) in aqueous buffer (10 mM acetate, pH 4.0). Samples were prepared by depositing a peptide solution (4 μL) onto a 200-mesh carbon-coated copper grid from Electron Microscopy Services (Hatfield, PA). After 90 s of incubation on the grid, the excess liquid was wicked away, leaving a thin film of sample. An aliquot (4 μL) of negative stain solution (1% uranyl acetate) was deposited onto the thin film. After 1 min of staining, the remaining moisture was wicked away, and the grid was dried overnight in a desiccator. Electron micrographs were captured on a Hitachi HT-7700 transmission electron microscopy, equipped with a tungsten filament and AMT CCD camera, operating at an accelerating voltage of 80 kV.
Wang F., Gnewou O., Modlin C., Beltran L.C., Xu C., Su Z., Juneja P., Grigoryan G., Egelman E.H, & Conticello V.P. (2021). Structural analysis of cross α-helical nanotubes provides insight into the designability of filamentous peptide nanomaterials. Nature Communications, 12, 407.
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3

Negative-Stain TEM Analysis of Glucagon Fibrils

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Negative-stain TEM images of the pH 2 glucagon fibrils were measured using an FEI Tecnai Spirit Bio-Twin Transmission Electron Microscope with an acceleration voltage of 120 kV. A 5 μl aliquot of the fibril solution was diluted 40-fold with water and mixed thoroughly. 5 μL of this diluted solution was deposited onto the surface of a 200 mesh carbon-coated copper grid (Electron Microscopy Sciences, Hatfield, PA). After 1 minute, excess liquid was blotted off using filter paper and the grid was rinsed briefly with 5 μL water. The rinse water was wicked away with filter paper and 5 μL 1% uranyl acetate was added to the grid as a negative stain to enhance contrast. After 1 minute, excess stain was blotted off and the grid was imaged immediately. Fibril width measurements were carried out using the program ImageJ.
Gelenter M.D., Smith K.J., Liao S.Y., Mandala V.S., Dregni A.J., Lamm M.S., Tian Y., Xu W., Pochan D.J., Tucker T.J., Su Y, & Hong M. (2019). The peptide hormone glucagon forms amyloid fibrils with two coexisting β-strand conformations. Nature structural & molecular biology, 26(7), 592-598.
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4

NP Sample Negative Staining for TEM

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The NP sample was mixed with acetate buffer (0.125 M CH3COONH4, 0.6 mM (NH4)2CO3 and 0.26 mM tetrasodium EDTA at pH 7.4). The sample (10 μl) was negatively stained with 10 μl of 2% (w/v) of phosphotungstic acid, cast on a 200-mesh carbon coated copper grid (Electron Microscopy Sciences) treated in NanoClean 1070, and dried in air. The TEM imaging was performed using a FEI Titan Themis 200 transmission electron microscope.
Banin E., Khare S.K., Naider F, & Rosenberg E. (2001). Proline-Rich Peptide from the Coral Pathogen Vibrio shiloi That Inhibits Photosynthesis of Zooxanthellae. Applied and Environmental Microbiology, 67(4), 1536-1541.
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5

Negative-Stain TEM Analysis of Glucagon Fibrils

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Negative-stain TEM images of the pH 2 glucagon fibrils were measured using an FEI Tecnai Spirit Bio-Twin Transmission Electron Microscope with an acceleration voltage of 120 kV. A 5 μl aliquot of the fibril solution was diluted 40-fold with water and mixed thoroughly. 5 μL of this diluted solution was deposited onto the surface of a 200 mesh carbon-coated copper grid (Electron Microscopy Sciences, Hatfield, PA). After 1 minute, excess liquid was blotted off using filter paper and the grid was rinsed briefly with 5 μL water. The rinse water was wicked away with filter paper and 5 μL 1% uranyl acetate was added to the grid as a negative stain to enhance contrast. After 1 minute, excess stain was blotted off and the grid was imaged immediately. Fibril width measurements were carried out using the program ImageJ.
Gelenter M.D., Smith K.J., Liao S.Y., Mandala V.S., Dregni A.J., Lamm M.S., Tian Y., Xu W., Pochan D.J., Tucker T.J., Su Y, & Hong M. (2019). The peptide hormone glucagon forms amyloid fibrils with two coexisting β-strand conformations. Nature structural & molecular biology, 26(7), 592-598.
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6

Preparation and Imaging of Peptide Samples for TEM

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Grids were prepared using diluted solutions of peptide (3 mg·mL−1) in aqueous buffer (10 mM acetate, pH 4.0). Samples were prepared by depositing 4 μL of peptide solution onto a 200-mesh carbon-coated copper grid from Electron Microscopy Services (Hatfield, PA). After 90 s of incubation on the grid, moisture was wicked away, leaving a thin film of sample. An aliquot (4 μL) of negative stain solution (1% uranyl acetate) was deposited onto the thin film. After 60 s of staining, the remaining moisture was wicked away, and the grid dried in a tabletop desiccator in vacuo for at least 5 min. Electron micrographs were recorded on a Hitachi HT-7700 transmission electron microscope with a tungsten filament and Advanced Microscopy Techniques charge-couupled device (CCD) camera at an accelerating voltage of 80 kV.
Wang F., Gnewou O., Wang S., Osinski T., Zuo X., Egelman E.H, & Conticello V.P. (2021). Deterministic chaos in the self-assembly of β sheet nanotubes from an amphipathic oligopeptide. Matter, 4(10), 3217-3231.
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7

Characterization of Nanoparticle Morphology

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Temperature- dependent DLS was performed on a NanoPlus (Particulate Systems, Norcross, GA). The temperature-dependent UV–vis spectra were collected on Cary 60 UV–vis spectrophotometer (Agilent Technologies). TEM images were acquired on a Hitachi H-7500 transmission electron microscope at an accelerating voltage of 75 kV. A 5–10 μL sample was dropped onto a 200-mesh carbon coated copper grid (Electron Microscopy Sciences) and incubated for 60 s following by wicking away the excess liquid. After 3 rounds of incubation, 5 μL of 1% methylamine tungstate (Ted Pella, Inc.) solution was added on the TEM gird to apply a negative stain on the OMA sample. After 60 s of incubation, the excess liquid was wicked away. For the AuNR sample, no negative staining is required. The sample grids were subsequently dried and stored in a desiccator. The magnification of the OMA particle image is 10k (Figure 2b), and the magnification of the AuNR image is 15 000× (Figure S13).
Zhao J., Su H., Vansuch G.E., Liu Z., Salaita K, & Dyer R.B. (2018). Localized Nanoscale Heating Leads to Ultrafast Hydrogel Volume-Phase Transition. ACS nano, 13(1), 515-525.
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8

Morphological Characterization and Genome Sequencing of Phage BK-30P

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For morphological characterization, purified phage particles were adsorbed onto 200-mesh carbon-coated copper grids (Electron Microscopy Sciences, Hatfield, PA, USA) and negatively stained with 2% uranyl acetate for 10 s. The stained phage particles were examined using a transmission electron microscope (CM200, Phillips, Eindhoven, The Netherlands) to analyze their morphology.
To extract the genomic DNA of BK-30P, it was sequenced at Macrogen Inc. using an Illumina Miseq system with 2 × 300 bp paired-end reads. The obtained raw data were assembled using SPAdes version 3.1.1 [31 (link)]. The Illumina platform provided 82-fold coverage of the genome. The genome was assembled into one contig through PCR-based gap closing.
Gene prediction in the genome was performed using a combination of two gene calling methods: the RAST server [25 (link)] and Genemark.hmm 3.25 [32 (link)]. The assignment of protein function to ORFs was performed manually using BLASTp against the NCBI nonredundant database and RPS-BLAST or HMMER search against the COG database [33 (link)], Pfam database [34 (link)], and TIGRFam database [35 (link)]. Furthermore, transmembrane helices were predicted using TMHMM [36 (link)], while the anticipation of signal peptides was conducted through SignalP [37 (link)].
Baek K, & Choi A. (2023). Macromonas nakdongensis sp. nov., Isolated from Freshwater and Characterization of Bacteriophage BK-30P—The First Phage That Infects Genus Macromonas. Microorganisms, 11(9), 2237.
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9

Visualizing and Characterizing Protein Fibrils

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For visualization of fibrils and characterization of the structure of the injected material, 5 mg/ml of PFFs was diluted 1:50 in PBS, after which 10 µl was adsorbed onto 200-mesh carbon-coated copper grids (Electron Microscopy Sciences, Hatfield, PA, USA), air dried for 5 min, and negative-stained by incubating with 10 µl of 2% uranyl acetate (Cat. Number U1006; Spectrum Chemical, Brunswick, NJ, USA) for 5 min. Fibrils were observed using a JEM-1400 transmission electron microscope (JEOUL; Akishima, Tokyo, Japan).
Pérez-Acuña D., Shin S.J., Rhee K.H., Kim S.J, & Lee S.J. (2023). α-Synuclein propagation leads to synaptic abnormalities in the cortex through microglial synapse phagocytosis. Molecular Brain, 16, 72.
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10

Structural Analysis of Fibril Morphology

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For visualization of fibrils and characterization of the structure of the injected material, 5 mg/ml PFFs were diluted 1:50 in PBS, after which 10 µl was adsorbed onto 200-mesh carbon-coated copper grids (Electron Microscopy sciences, Hatfield, PA, USA), air dried for 5 min, and negative stained by incubating with 10 µl of 2% uranyl acetate (Cat. Number U1006, Spectrum Chemical, Brunswick, NJ, USA) for 5 min. Fibrils were observed using a JEM-1400 transmission electron microscope (JEOUL, Akishima, Tokyo Japan).
Pérez-Acuña D., Rhee K.H., Shin S.J., Ahn J., Lee J.Y, & Lee S.J. (2023). Retina-to-brain spreading of α-synuclein after intravitreal injection of preformed fibrils. Acta Neuropathologica Communications, 11, 83.
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