Cm10 electron microscope

Manufactured by Philips

Sourced in Netherlands, United States

The Philips CM10 electron microscope is a versatile laboratory instrument designed for high-resolution imaging and analysis of microscopic samples. It utilizes an electron beam to produce magnified images, enabling detailed examination of a wide range of materials and structures at the nanoscale level.

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Lab products found in correlation

Image pro plus software, by Media Cybernetics (3 mentions) Ultracut r ultramicrotome, by Leica camera (2 mentions) Ultramicrotome, by Reichert Technologies (2 mentions) Glutaraldehyde, by Polysciences (2 mentions) Epon 812, by Serva Electrophoresis (2 mentions) Biotinylated goat anti rabbit igg, by Vector Laboratories (2 mentions) H 029 30, by Phoenix Pharmaceuticals (2 mentions) Liquid release coated slides, by Electron Microscopy Sciences (2 mentions) Abc elite kit, by Vector Laboratories (2 mentions) Tecnai t12 electron microscope, by Thermo Fisher Scientific (2 mentions) Glow discharged continuous carbon grid, by Electron Microscopy Sciences (2 mentions) Poly bed, by Polysciences (2 mentions) Item software, by Olympus (2 mentions) Araldite, by Merck Group (2 mentions) Matrigel, by Thermo Fisher Scientific (2 mentions) Lead citrate, by Merck Group (2 mentions) Glutaraldehyde, by Merck Group (2 mentions) Axiovert 200m, by Zeiss (2 mentions) Ultrascan digital camera, by Ametek (1 mentions) Tecnai g2, by Thermo Fisher Scientific (1 mentions)

135 protocols using cm10 electron microscope

Structural Analysis of TopIIIα-RMI1 Complex

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Sample used for crystal growth was diluted to a concentration of 200 nM in 25 mM HEPES pH 7.4, 100 mM NaCl and 0.2 mM TCEP immediately before applying it to glow-discharged holey carbon grids (Cu 400 mesh grids, Quantifoil Micro Tool GmbH). The protein was adsorbed to the EM grids for 45 seconds and negatively stained with 2% (m/w) uranyl acetate solution. The grid was examined using a Philips CM10 electron microscope equipped with a LaB6 filament and operated at 80 kV. Images were recorded as CCD micrographs at 130000× nominal magnification resulting in a pixel size of 3.7 Å. A total of 4000 particles were picked and subsequently analyzed using EMAN2. To avoid model bias, the initial model used for angular refinements was a featureless Gaussian blob with dimension estimated from the crystal structure of TopIIIα-RMI1, generated with the command makeinitialmodel.py as implemented in EMAN. After several cycles of refinement convergence to the final model shown in Supplementary fig. 3 was attained. The angular spacing used for orientation generation was set to 10 deg. Smaller increment did not improve the model further.

Bocquet N., Bizard A.H., Abdulrahman W., Larsen N.B., Faty M., Cavadini S., Bunker R.D., Kowalczykowski S.C., Cejka P., Hickson I.D, & Thomä N.H. (2014). Structural and mechanistic insight into Holliday junction dissolution by Topoisomerase IIIα and RMI1. Nature structural & molecular biology, 21(3), 261-268.

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Platelet Dense Granule Enumeration by EM

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Acid citrate dextrose (ACD) tubes of blood were obtained to evaluate platelet dense granule numbers by EM.^{21 (link)} One tube was processed immediately for a whole mount preparation of air-dried platelets; the second vial was shipped with the frozen PFP aliquots but packaged to ensure these vials remained at ambient temperature and subsequently processed for EM 48 hours postvenipuncture. Preparations of platelet whole mounts required low-speed centrifugation to obtain platelet-rich plasma, which was subsequently incubated upon EM support films for 5 minutes followed by a brief distilled water wash and then air-dried.^{22 (link)} Enumeration of δ-granules using a Philips CM 10 electron microscope was performed; the average number of δ-granules was determined by counting the total number of 100 platelets contiguously observed, excluding platelets that were obscured by debris or partially overlaying grid bars.^{23 (link)}

Mai D.B., Smith M.R, & Gunning WT I.I.I. (2018). Assessment of the Stability of von Willebrand Profile Clotting Factors and Platelet Dense Granule Testing Following Air Transport. Clinical and Applied Thrombosis/Hemostasis, 24(8), 1261-1266.

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Electron Microscopy of Cultured Cells

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Cells, grown in flasks, were rinsed in 0.15 M phosphate buffer (pH 7.4), were fixed in situ with 2.5% glutaraldehyde for 40 minutes, and then they were gently scraped, centrifuged and post-fixed in 1% OsO 4 for 1 hour. Pellets were dehydrated, using increasing concentrations of ethanol, and embedded in araldite.
Ultrathin sections were stained with uranyl acetate and lead citrate and then analyzed using a Philips CM10 electron microscope (Battistelli et al., 2011; (link)Burattini et al., 2013) .

Salucci S., Baldassarri V., Canonico B., Burattini S., Battistelli M., Guescini M., Papa S., Stocchi V, & Falcieri E. (2016). Melatonin behavior in restoring chemical damaged C2C12 myoblasts. Microscopy research and technique, 79(6).

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Ultrastructural Analysis of Brain Microvessels

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The effects of ATDC5 on the tight junctions of brain microvessels were also examined using transmission electron microscopy (TEM). For these studies, the mice received an injection of either a vehicle (PBS) or 0.01 mmol/kg of ADTC5. The mice were then sacrificed and perfused with 3% glutaraldehyde in 0.1 M Sorensen’s phosphate buffer (pH 7.3) at 2 h and 4 h. Various organs including the brain were removed and fixed in 3% glutaraldehyde in 0.1 M Sorensen’s phosphate buffer followed by postfixation in 1% osmium tetroxide in 0.1M Sorensen’s phosphate buffer. Tissues were then dehydraded and embedded in Epon 812 using standard techniques. The sections were stained with uranyl acetate and lead citrate, and examined using a Philips CM 10 electron microscope.

Laksitorini M.D., Kiptoo P.K., On N.H., Thliveris J.A., Miller D.W, & Siahaan T.J. (2015). Modulation of Intercellular Junctions by Cyclic-ADT Peptides as a Method to Reversibly Increase Blood-Brain Barrier Permeability. Journal of pharmaceutical sciences, 104(3), 1065-1075.

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Immunolocalization of FOP1 using GFP

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For immuno-EM, a C-terminal FOP1:GFP fusion under endogenous expression was prepared for immuno-EM using high-pressure freezing and freeze substitution (Dahl and Staehelin, 1989 (link); Meehl et al., 2009 (link)). Incubation in rabbit-generated α-GFP antibodies, followed by incubation with α-rabbit secondary antibodies conjugated to 15-nm gold particles was used to localize Fop1-GFP. Fop1 was then localized in 60-nm sections by transmission EM. Images were acquired using a CM10 electron microscope (Philips) with a BioScan2 CCD camera (Gatan). For EM analysis of FOP1 knockdown BB structural defects, FOP1 knockdown cells were subjected to high-pressure freezing and freeze substitution as previously described (Pearson et al., 2009 (link)). Images were acquired using a Tecnai G2 (FEI) equipped with a Gatan Ultrascan digital camera. All images were processed for figures using Corel Draw.

Bayless B.A., Galati D.F., Junker A.D., Backer C.B., Gaertig J, & Pearson C.G. (2016). Asymmetrically localized proteins stabilize basal bodies against ciliary beating forces. The Journal of Cell Biology, 215(4), 457-466.

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Ultrastructural Analysis of Drosophila Muscle

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Sample preparation and image acquisition were performed essentially as previously described52 (link). In brief, fillets were fixed with 4% PFA (in PBS) for 10 min at room temperature followed by fixation in 2.5% glutaraldehyde (in PBS) overnight at 4 °C. Next, samples were treated with 1% osmium tetroxide in 100 mM phosphate buffer, pH 7.2, for 1 h on ice. Larval fillets were rinsed with water, treated with 1% aqueous uranyl acetate (UA) for 1 h at 4 °C, dehydrated through a graded series of ethanol concentrations, and stored in liquid Epon overnight. Next, muscles 4 of segment 4 were dissected with sharp insect pins, embedded in Epon, and polymerized for 48 h at 60 °C. Ultrathin sections were stained with UA and lead citrate and viewed in a Philips CM10 electron microscope.

Zhang Y.V., Hannan S.B., Kern J.V., Stanchev D.T., Koç B., Jahn T.R, & Rasse T.M. (2017). The KIF1A homolog Unc-104 is important for spontaneous release, postsynaptic density maturation and perisynaptic scaffold organization. Scientific Reports, 7, 38172.

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Ultrastructural Analysis of Dorsal Root

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WT and Zfp106^−/− littermates were perfused as above (3% glutaraldehyde in 0.05 M sodium cacodylate) and dorsal roots dissected. Ultrathin sections 80 nm thick were cut from selected areas of the tissue, stained with uranyl acetate and lead citrate, and examined at 80 kV in a Philips CM10 electron microscope. Images were taken using a Megaview 3 digital camera and Olympus iTEM software. Morphology was analysed from 15-week-old WT and Zfp106^−/− littermates (female, n = 3 per genotype).

Joyce P.I., Fratta P., Landman A.S., Mcgoldrick P., Wackerhage H., Groves M., Busam B.S., Galino J., Corrochano S., Beskina O.A., Esapa C., Ryder E., Carter S., Stewart M., Codner G., Hilton H., Teboul L., Tucker J., Lionikas A., Estabel J., Ramirez-Solis R., White J.K., Brandner S., Plagnol V., Bennet D.L., Abramov A.Y., Greensmith L., Fisher E.M, & Acevedo-Arozena A. (2015). Deficiency of the zinc finger protein ZFP106 causes motor and sensory neurodegeneration. Human Molecular Genetics, 25(2), 291-307.

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Ultrastructural Analysis of C. elegans Nuclei

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Young adult nematodes were prepared for transmission electron microscopy by high-pressure freezing and freeze substitution following standard methods for ultrastructure (Hall et al., 2012 (link)). unc-4(e120) worms served as controls. After embedding into plastic resin, lengthwise thin sections were collected with a RMC Powertome (Boeckler Instruments, Tucson, AZ) onto Formvar-coated slot grids for inspection with a Philips CM10 electron microscope. Digital images were collected with an Olympus SIS Morada camera system and analyzed using iTEM software and Photoshop. Montages of low-power images were used to document the layout of tissues in each animal, and then higher-power images were used to determine the morphology of the nuclear membrane and localization of P-granules. All quantification was done on individual cross-sectional images of nuclei.

VanGompel M.J., Nguyen K.C., Hall D.H., Dauer W.T, & Rose L.S. (2015). A novel function for the Caenorhabditis elegans torsin OOC-5 in nucleoporin localization and nuclear import. Molecular Biology of the Cell, 26(9), 1752-1763.

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Negative Staining and Electron Microscopy of αIIbβ3–Abciximab Complex

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4-μL aliquots of the αIIbβ3–abciximab complex (0.01 mg/mL) were adsorbed for 30 s onto glow-discharged copper grids covered with a carbon-coated plastic film and negatively stained with 0.75% (w/v) uranyl formate solution as described.^{25 (link)} Specimens were imaged with a CM10 electron microscope (Philips) equipped with a tungsten filament and operated at an acceleration voltage of 100 kV. Micrographs were collected with an XR16L-ActiveVu camera (AMT) at a defocus value of −1.5 μm. The nominal magnification was 52,000X, which corresponds to a calibrated magnification of 41,513X and a pixel size of 2.65 nm at the specimen level. From 49 images, 14,593 particles were automatically picked with Gautomatch (http://www.mrc-lmb.cam.ac.uk/kzhang/Gautomatch/) and windowed into 128X128-pixel images. After image normalization and particle centering, the particle images were classified into 100 groups using K-means classification procedures implemented in SPIDER.^{26 (link)}

Nešić D., Zhang Y., Spasic A., Li J., Provasi D., Filizola M., Walz T, & Coller B.S. (2020). Cryo-Electron Microscopy Structure of the αIIbβ3–Abciximab Complex. Arteriosclerosis, thrombosis, and vascular biology, 40(3), 624-637.

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Preparing Adult Animals for Electron Microscopy

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Adult animals were prepared for electron microscopy by standard methods [Hall, 1995 (link)]. Briefly, live animals were rinsed in M9 buffer and cut open using a razor blade in buffered aldehydes, rinsed in buffer and re-fixed in buffered osmium tetroxide, then rinsed in buffer and en bloc stained in uranyl acetate before dehydration and embedding in plastic resin. Thin sections were collected onto Formvar-coated slot grids, re-stained with uranyl acetate and/or lead citrate, then viewed with a Philips CM10 electron microscope. Images were collected on film, or using an Olympus Morada digital camera system.

Qadota H., Matsunaga Y., Nguyen K.C., Mattheyses A., Hall D.H, & Benian G.M. (2017). High resolution imaging of muscle attachment structures in C. elegans. Cytoskeleton (Hoboken, N.J.), 74(11), 426-442.

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