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Ultra 897 emccd

Manufactured by Oxford Instruments
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The Ultra 897 EMCCD is a high-performance electron-multiplying charge-coupled device (EMCCD) camera designed for scientific imaging applications. It features a large sensor, low-noise electronics, and advanced on-chip electron multiplication, enabling the capture of high-quality images with exceptional sensitivity even in low-light conditions.

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Lab products found in correlation

A1r laser scanning confocal microscope, by Oxford Instruments (2 mentions) Focalcheck test slide, by Thermo Fisher Scientific (2 mentions) Nstorm system, by Oxford Instruments (1 mentions)

Spelling variants of this product

Ultra 897 EMCCD camera (36 citations) Ultra 897 (34 citations) IXon Ultra 897 EMCCD camera (33 citations) IXon Ultra 897 EMCCD (14 citations) IXon Ultra DU-897 EMCCD camera (6 citations) Ultra DU-897 EMCCD camera (4 citations) Andor 897 Ultra EMCCD camera (3 citations) Andor iXon Ultra 897 EMCCD camera (3 citations) 897 ultra backilluminated EMCCD (2 citations) IXon Ultra 897 EMCCD Andor Cameras (2 citations)

8 protocols using ultra 897 emccd

1

Imaging Printed Nanocomposites with Inverted Microscope

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The printed nanocomposites were imaged using a homebuilt inverted microscope equipped with an oil immersion objective (Nikon Plan Apo VC, 100×, numerical aperture = 1.4; oil: Cargille Immersion Oil Type FF, lot: 010780; n = 1.479), a tube lens (f = 200 mm), and an electron-multiplying charge-coupled device (EMCCD) camera (Andor iXon Ultra 897 EMCCD; T = −60°C). Specifically, samples printed using a 50-μm nozzle on glass coverslip were excited using a 405-nm continuous-wave diode laser (Thorlabs LP405-SF30), and their fluorescence (emission, ~515 nm) was passed through a dichroic mirror (Semrock FF414-Di01-25x36) and additional long-pass and bandpass filters to reduce the background signal (Semrock FF02-409/LP-25 and Thorlabs FB500-40). Nanowires within the printed nanocomposites were focused on, and then an additional lens (f = 250 mm) was added to the optical path between the objective and tube lens to image the Fourier space, as described previously (36 (link)). The exposure time was 2 to 3 s for each image, and the camera was operated in “conventional” mode (readout rate, 3 MHz). Further details and schematics are provided in fig. S8.
Zhou N., Bekenstein Y., Eisler C.N., Zhang D., Schwartzberg A.M., Yang P., Alivisatos A.P, & Lewis J.A. (2019). Perovskite nanowire–block copolymer composites with digitally programmable polarization anisotropy. Science Advances, 5(5), eaav8141.
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2

Correlative Fluorescence and Electron Microscopy

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Localization fluorescence microscopy was performed in blinking buffer (10% w/v glucose, 0.8 mg/mL Glucose oxidase, 0.04 mg/mL Catalase, 100mM 2-mercaptoethanol made fresh in PBS immediately before imaging) in a sealed chamber. Imaging was performed on a Nikon NSTORM system equipped with an Andor iXon Ultra 897 emccd. Prior to localization imaging, a 15×15 large image montage covering approximately 1 mm2 was acquired with 488 nm and with 647 nm epifluorescence excitation. This created a map of all cells in the region (488 nm) and which cells were expressing the target protein (647 nm). It also allowed visualization of the quality of unroofing. Localization microscopy was performed on 6–11 regions (256 × 256 pixels) with 10 kW/cm2, 647 nm laser in deep TIRF or highly inclined (HiLo) illumination, 10 ms frames, for 25000 to 45000 frames. After localization imaging and marking each region onto the large montage map, the bottom of coverslip was etched with a 4 mm diameter circle using a diamond objective marker (Leica 11505059). This etched circle is the region that is subsequently processed for electron microscopy. The oil was cleaned off the coverslip, rinsed with PBS and stored in 2% glutaraldehyde at 4 °C for a minimum of 1 hour and a maximum of 24 hours.
Sochacki K.A., Dickey A.M., Strub M.P, & Taraska J.W. (2017). Endocytic proteins are partitioned at the edge of the clathrin lattice in mammalian cells.. Nature cell biology, 19(4), 352-361.
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3

Optogenetic Cardiac Electrophysiology Mapping

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Cell monolayers infected with Ad-CMV-hChR2(H134R)-eYFP (MOIs 25 and 250, respectively) or AAV9.CAG.hChR2(H134R)-mCherry.WPRE.SV40 (MOI 50,000–100,000 ± 500 mU/mL NM) were stained with the calcium- and voltage-sensitive dyes and optically mapped using our recently published all-optical, high-throughput system for dynamic cardiac electrophysiology, termed OptoDyCE (Klimas et al., 2016 (link), 2018 (link)). The excitation filter for the actuating LED was 470/28 nm, the LED illumination for the voltage (di-4-ANBDQBS or Berst1) and calcium (Rhod-4AM) measurements was filtered as follows: 655/40 nm and 535/50, respectively. Fluorescence was collected by iXon Ultra 897 EMCCD; Andor, after passing through the emission filter 595/40 nm+700LP. Note that the UPenn Core considers the CAG and the CB7 promoters equivalent and uses them interchangeably; both are ubiquitous promoters, derivatives of CMV (Miyazaki et al., 1989 (link)).
Ambrosi C.M., Sadananda G., Han J.L, & Entcheva E. (2019). Adeno-Associated Virus Mediated Gene Delivery: Implications for Scalable in vitro and in vivo Cardiac Optogenetic Models. Frontiers in Physiology, 10, 168.
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4

Formation and Characterization of Rhodamine-Labeled GUVs

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DOPC+0.2mol% rhodamine-DPPE were prepared by mixing appropriate amount of lipid stock solutions. After depositing onto ITO coated glass slides, lipid dry films were vacuumed for > 2 h to remove organic solvents. A GUV production chamber filled with 100 mM sucrose and 10 mM HEPES (pH 7.4) was formed by sealing lipid dry films with a Viton O-ring. The assemblage was heated to 60°C using a Digi-Sense temperature controller. GUVs were generated by lipid swelling under an AC field of 10 Hz and 2.0 Volt (duration of 2 h). GUV solution was transferred to 3 mL buffer containing 100 mM glucose and 10 mM HEPES (pH 7.4). After settling for > 1 h, GUV aliquot from the bottom was transferred onto a coverslip and examined by fluorescence microscopy using a Nikon Eclipse-U microscope and an Andor iXon Ultra 897 EM-CCD. To retard liquid evaporation, the cover slip was housed in a homemade hollow chamber sealed by copper plates and thermal insulation foam. To study the effect of polyQ35 aggregates, an equal volume of peptide solution (after adjusting glucose concentration to 100 mM) was mixed with a GUV aliquot (final peptide concentration was 15 μM). Immediately after mixing, time-lapse or single-shot fluorescence micrographs were collected. Control experiments were performed by mixing buffer-only solution with the GUV aliquot.
Ho C.S., Khadka N.K., She F., Cai J, & Pan J. (2016). Polyglutamine Aggregates Impair Lipid Membrane Integrity and Enhance Lipid Membrane Rigidity. Biochimica et biophysica acta, 1858(4), 661-670.
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5

3D Super-Resolution Imaging Protocol

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3D‐STORM was performed as previously described.[22] In brief, samples were mounted on glass slides using a standard STORM imaging buffer consisting of 5% (w/v) glucose, 100 × 10−3m cysteamine, 0.8 mg mL−1 glucose oxidase, and 40 µg mL−1 catalase in Tris‐HCl (pH 7.5). A cylindrical lens was inserted into the imaging path to introduce astigmatism so that images of single molecules were elongated in opposite directions for molecules on the proximal and distal sides of the focal plane. Data was collected at 110 frames per second using an Andor iXon Ultra 897 EM‐CCD, for a total of ≈50 000 frames per image. 3D‐STORM raw data were processed according to previously described methods.[22]
Xing F., Dong H., Yang J., Fan C., Hou M., Zhang P., Hu F., Zhou J., Chen L., Pan L, & Xu J. (2023). Mesenchymal Migration on Adhesive–Nonadhesive Alternate Surfaces in Macrophages. Advanced Science, 10(23), 2301337.
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6

Confocal Imaging of HLB Puncta

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Following immunofluorescent staining, cells were imaged using a Nikon A1R Laser Scanning Confocal microscope equipped with an Andor iXon 897 Ultra EMCCD and NIS Elements software (v. 5.30). Cells with detectable HLB puncta were selected using a 10× NA 0.45 air objective and their XY coordinates were saved. Individual Z-stacks of selected cells were then captured sequentially using a Plan Apo λ 100×1.45 NA oil objective with 0.1 μm step size and 1.0 AU pinhole size per channel. Chromatic aberration between the TRITC and Cy5 channels was quantified using 0.5 μm fluorescent microspheres on a FocalCheck test slide (Invitrogen, F36909). The Cy5 channel was computationally shifted by +0.06 μm in the X plane for all nuclear Z-stacks to compensate for the measured aberration.
, & Kato Y. (1995). The future of voice-processing technology in the world of computers and communications.. Proceedings of the National Academy of Sciences of the United States of America, 92(22), 10060-10063.
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7

TIRF Microscopy of Microtubule Dynamics

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10% Alexa 488-labeled tubulin was assembled onto 10% TAMRA-labeled microtubule seeds and imaged by TIRF microscopy as previously described [41 (link), 42 (link)]. Briefly, to keep the microtubules within the excitation field, the microtubule seeds polymerized by GMPCPP were attached to a cover glass surface coated with anti-TAMRA antibody. Microtubules were polymerized with Alexa 488-labeled and unlabeled tubulin (1:9) from the GMPCPP-stabilized and TAMRA-labeled microtubule seeds in the presence of 1 mm GTP and the indicated concentrations of FOR20. The mixture was incubated in image buffer for 5 min at 35 °C and then introduced into the imaging chamber in the IX83HB constant temperature incubator (Olympus IX83-ZDC microscope, Shinjuku, Tokyo, Japan) to observe microtubule dynamics. The image buffer consisted of BRB80 supplemented with 2 mm GTP, 80 mmd-glucose, 0.4 mg ml−1 glucose oxidase, 0.2 mg ml−1 catalase, 0.8 mg ml−1 casein, 1% β-Mercaptoethanol, 0.001% Tween-20. Images were collected with an Andor 897 Ultra EMCCD (Andor, Belfast, UK) using a 100X/1.45 NA TIRF objective. Images with 100 ms exposure time were recorded every 2.5 s, 488 and 561 nm lasers were used to excite the fluorescent labels.
Feng S., Song Y., Shen M., Xie S., Li W., Lu Y., Yang Y., Ou G., Zhou J., Wang F., Liu W., Yan X., Liang X, & Zhou T. (2017). Microtubule-binding protein FOR20 promotes microtubule depolymerization and cell migration. Cell Discovery, 3, 17032-.
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8

Confocal Imaging of HLB Puncta

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Following immunofluorescent staining, cells were imaged using a Nikon A1R Laser Scanning Confocal microscope equipped with an Andor iXon 897 Ultra EMCCD and NIS Elements software (v. 5.30). Cells with detectable HLB puncta were selected using a 10× NA 0.45 air objective and their XY coordinates were saved. Individual Z-stacks of selected cells were then captured sequentially using a Plan Apo λ 100×1.45 NA oil objective with 0.1 μm step size and 1.0 AU pinhole size per channel. Chromatic aberration between the TRITC and Cy5 channels was quantified using 0.5 μm fluorescent microspheres on a FocalCheck test slide (Invitrogen, F36909). The Cy5 channel was computationally shifted by +0.06 μm in the X plane for all nuclear Z-stacks to compensate for the measured aberration.
Armstrong C., Passanisi V.J., Ashraf H.M, & Spencer S.L. (2023). Cyclin E/CDK2 and feedback from soluble histone protein regulate the S phase burst of histone biosynthesis. Cell reports, 42(7), 112768.
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