So 163

Manufactured by Kodak

Sourced in United States

The SO-163 is a piece of laboratory equipment manufactured by Kodak. It is designed for use in various scientific and industrial applications. The core function of the SO-163 is to perform specific tasks within the laboratory environment.

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Lab products found in correlation

Jem 100s, by JEOL (1 mentions) Cp3 plunge freezing device, by Ametek (1 mentions) Super coolscan 9000 ed scanner, by Nikon (1 mentions) Ammonium molybdate, by Merck Group (1 mentions) Jem 100cx electron microscope, by Kodak (1 mentions) Jem 1200ex electron microscope, by JEOL (1 mentions) Mark 4, by Thermo Fisher Scientific (1 mentions)

7 protocols using so 163

Cryo-EM of Rotavirus A-Capsids

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An aliquot (3 µl) of RRV A-capsids was applied to a Quantifoil R2/1 grid, blotted, and plunge-frozen. Focal-pair images were recorded on Kodak SO163 films at 300kV with a magnification of 33,000 and an electron dose of ~10 electrons/Å²/micrograph. Films were digitized in a Zeiss SCAI densitometer using a step size equivalent to 2.1 Å/pixel on the specimen.
Data processing was carried outwith IMIRS (Liang et al., 2002 (link)) with modifications (Liu et al., 2008 (link)). We boxed out 22,889 particle images from 320 micrographs and included 14,374 particles in the final reconstruction. The effective resolution, 7.2Å, is based on the Fourier shell correlation (FSC) criterion of 0.143 (about 8.5 Å at 0.5 FSC) (Rosenthal and Henderson, 2003 (link)) between two maps from half datasets independently processed and reconstructed (Fig. S1a).

Zhou Z.H., Hui W.H., Shah S., Jih J., O’Connor C.M., Sherman M.B., Kedes D.H, & Schein S. (2014). Four levels of hierarchical organization including non-covalent chainmail brace the mature tumor herpesvirus capsid against pressurization. Structure (London, England : 1993), 22(10), 1385-1398.

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Ultrastructural Analysis of Synaptic Profiles

Cited 2 times

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Ultrastructure was analyzed with two electron microscopes (EM). One EM is a JEOL JEM 100S transmission electron microscope with which areas of interest were photographed at 15,000–40,000 magnification with high-resolution film (Kodak SO-163; Kodak, Rochester, NY, USA). The negatives were scanned at 1200–2000 pixels/inch (ScanMaker 800, Microtek, Santa Fe Springs, CA, USA) to produce digital images. A second EM is a Phillips CM10 equipped with a digital camera for direct capture of digital images. Synapses were identified by the presence of vesicles in the presynaptic profile, a clear synaptic cleft and the presence of a postsynaptic density. Tracer-labeled profiles were readily identified by the presence of DAB precipitate. GABA-positive (GABA+) profiles were easily distinguished from GABA-negative profiles by a distinct difference in the density of overlying gold particles (Nakamoto et al., 2013a (link)). GABA immunostaining was also readily distinguished from the DAB label (Nakamoto et al., 2013b (link)).

Mellott J.G., Bickford M.E, & Schofield B.R. (2014). Descending projections from auditory cortex to excitatory and inhibitory cells in the nucleus of the brachium of the inferior colliculus. Frontiers in Systems Neuroscience, 8, 188.

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Cryo-EM imaging of PCV2 virus

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A 3 μl aliquot of the PCV2 sample at 3 mg/ml concentration was applied to 400-mesh holey carbon grids (1.2/1.3 C-flat, Protochips). After blotting excessive sample solution, the grid was plunge frozen in liquid ethane cooled by liquid nitrogen using the Cp3 plunge-freezing device (Gatan). Cryo-EM images were taken using a FEI Titan Krios electron cryo-microscope with field emission gun (FEG) operated at 300 kV and parallel illumination. The images were recorded on Kodak SO163 negative films at low dose (25–27 e/Å²) and at a nominal magnification of 59k with intended defocus range of 1.5–2.5 μm. The films without obvious ice contamination (141 out of 168) were selected for digitization using a Nikon Super CoolScan 9000ED scanner with step size of 6.35 μm/pixel. The final calibrated sampling of the scanned images is 1.08 Å/pixel.

Liu Z., Guo F., Wang F., Li T.C, & Jiang W. (2016). 2.9 Å Resolution Cryo-EM 3-D Reconstruction of Close-packed Virus Particles. Structure (London, England : 1993), 24(2), 319-328.

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High-Voltage Electron Microscopy Tomography

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The grid with the ice-embedded cells was set on a cryo-specimen holder for HVEM (Gatan Inc. Pleasanton, CA, USA) precooled with liquid nitrogen to –150 °C. They were then transferred into a high-voltage H-1250M electron microscope (Hitachi Co. Ltd., Tokyo, Japan) operated at 1 MV accelerating voltage. The tilt series were collected from −60° to +60° in 3° steps. The images were recorded at a magnification of ×10,000 on electron films (Kodak SO-163) with a low electron dose to minimize specimen damage. Underfocus of 6 to 10 μm was used. The negatives were developed with full-strength D-19 developer (Kodak) for 12 min and subsequently digitized using a Coolscan 9000ED flatbed scanner (Nikon Co. Ltd., Tokyo, Japan) at a resolution of 4000 dpi. The image data were finally reduced in size by using a median filter with binning 2, representing a resolution of 1.27 nm/pixel.

Murata K., Hagiwara S., Kimori Y, & Kaneko Y. (2016). Ultrastructure of compacted DNA in cyanobacteria by high-voltage cryo-electron tomography. Scientific Reports, 6, 34934.

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Exosome Visualization via Negative Staining

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BHY and FaDu exosomes (isolated from 3 ml conditioned medium) were absorbed onto glow discharged carbon coated grids (G2400C from Plano) for 2 minutes. The solution was blotted of and negatively stained with 4% ammonium molybdate (Sigma-Aldrich) solution for 30 seconds. Micrographs were recorded with a Jeol JEM 100CX electron microscope at 100 kV onto Kodak SO163 film. Negatives were digitized with a Hasselblad Flextight × 5 scanner at 3000 dpi, resulting in a pixel size of 0.25 nm/px. For visualization images were binned to 1 nm/px.

Mutschelknaus L., Azimzadeh O., Heider T., Winkler K., Vetter M., Kell R., Tapio S., Merl-Pham J., Huber S.M., Edalat L., Radulović V., Anastasov N., Atkinson M.J, & Moertl S. (2017). Radiation alters the cargo of exosomes released from squamous head and neck cancer cells to promote migration of recipient cells. Scientific Reports, 7, 12423.

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Electron Microscopy Analysis of Protein Complexes

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BPaS1 preparations (0.8 mg/mL) in buffered conditions with 50 mM TrisHCl, pH 8.0; 100 mM NaCl; 10 mM MgCl2; 5 mM β-mercaptoethanol, as well as peptides (0.5 mg/mL) in buffer conditions, 50 mM TrisHCl, pH 7.5; 150 mM NaCl was analyzed using a JEM-1200EX electron microscope (JEOL, Tokyo, Japan) according to the method used previously [46 (link)]. Before analysis, the concentration of drugs was adjusted with the appropriate buffer to 0.2 mg/mL. Samples were prepared for negative contrast analysis. A copper mesh (400 Mesh, Electron Microscopy Sciences, Hatfield, PA, USA) coated with a formvar film (0.2% (weight/volume) formvar solution in chloroform) was placed on a drop of the preparation (~10 μL). After adsorption (5 min), the meshes with the preparation were transferred to a 1% (weight/volume) aqueous solution of uranyl acetate (1 min). The analysis of the preparations was carried out at an accelerating voltage of 80 kV. The shooting was carried out on Kodak film (SO-163) for EM at a magnification of 40,000.

Grishin S.Y., Dzhus U.F., Glukhov A.S., Selivanova O.M., Surin A.K, & Galzitskaya O.V. (2021). Identification of Amyloidogenic Regions in Pseudomonas aeruginosa Ribosomal S1 Protein. International Journal of Molecular Sciences, 22(14), 7291.

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Negatively Stained and Vitrified Specimen Preparation

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To prepare negatively stained specimens, 5 μL samples were applied to carbon-coated EM grids, rendered hydrophilic by glow discharge, and stained using 1–2%(w/v) uranyl acetate solutions. To prepare vitrified specimens, 5 μL samples were applied to perforated carbon EM grids (Quantifoil) that had been glow discharged in the presence of n-amylamine. Grids were blotted and plunged into a slush of liquid ethane using a semi-automated vitrification system (Vitrobot Mark IV, FEI) at 4 °C and 90–100% relative humidity. All images were recorded using a Phillips Tecnai T12 microscope, equipped with a LaB6 filament, and operated at 120 kV. Cryo-EM images of the tubes were recorded on SO-163 (Kodak) film at a nominal magnification of 42000x, at 1–2 μm underfocus. Selected images were digitized using a Nikon LS-9000 film scanner at a raster step size of 10.5 μM, corresponding to 2.5 Å on the specimen.

Jaballah S.A., Bailey G.D., Desfosses A., Hyun J., Mitra A.K, & Kingston R.L. (2017). In vitro assembly of the Rous Sarcoma Virus capsid protein into hexamer tubes at physiological temperature. Scientific Reports, 7, 2913.

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