Orca flash 4.0 c11440

Manufactured by Hamamatsu Photonics

Sourced in Japan

The Orca Flash 4.0 C11440 is a scientific CMOS (sCMOS) camera designed for high-speed, high-resolution imaging applications. It features a 4.2-megapixel sensor with a pixel size of 6.5 μm and a maximum frame rate of 100 fps. The camera offers a dynamic range of 16 bits and is capable of capturing images with low noise and high sensitivity.

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Lab products found in correlation

Eclipse ti, by Nikon (4 mentions) Ix83 inverted microscope, by Olympus (2 mentions) Nm band pass filter, by IDEX Corporation (2 mentions) Aquacosmos imaging station, by Hamamatsu Photonics (2 mentions) Hcimage software, by Hamamatsu Photonics (2 mentions) Observer z1, by Zeiss (1 mentions) Alexa fluor 546, by Thermo Fisher Scientific (1 mentions) Cytation 5 imaging reader, by Agilent Technologies (1 mentions) Alexa fluor 488, by Thermo Fisher Scientific (1 mentions) 4 6 diamidino 2 phenylindole (dapi), by Merck Group (1 mentions) Plan apo λ 60x oil objective, by Nikon (1 mentions) Tetraspeck microsphere, by Thermo Fisher Scientific (1 mentions) Eclipse ti2 microscope, by Nikon (1 mentions) Ixon ultra camera, by Oxford Instruments (1 mentions) Plan apo, by Nikon (1 mentions) Fv1000, by Olympus (1 mentions) Uplansapo, by Olympus (1 mentions)

13 protocols using orca flash 4.0 c11440

Simultaneous Imaging of Cells and Nanomaterials

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To simultaneously track cells and nanomaterials using SEPC, an Olympus ix83 inverted microscope, with phase contrast plate, was retrofitted with an oblique angle LED ring illuminator (Amscope LED-144-YK ring lamp), which attached to the microscopes brightfield condenser. Using this ring LED setup, we were able to achieve longer condenser (~3 cm) working distances as compared to traditional setups which take the place of the brightfield condenser. Typical LED powers were between 20%−50% of maximum power (Fig S6).
For phase contrast microscopy, LUCPlanFLNPh 20× and 40× objectives were used. With a numerical aperture (NA) of 0.4 and 0.65 respectively. The relatively low NA cut down on background scattering, allows for a clear DF image. For live cell imaging an Air-Therm ATX-H thermal heater coupled to a Precision Plastics stage top incubator was employed, maintaining physiological conditions (i.e. 95% humidity, 37°C internal temperatures, pH = 7.4).
Images were recorded on a Hamamatsu Orca Flash 4.0 C11440 at 16bit depth with a 0.16 μm to 0.33 μm pixel resolution.

Zimmerman J.F., Ardoña H.A., Pyrgiotakis G., Dong J., Moudgil B., Demokritou P, & Parker K.K. (2019). Scatter Enhanced Phase Contrast Microscopy for Discriminating Mechanisms of Active Nanoparticle Transport in Living Cells. Nano letters, 19(2), 793-804.

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Bacteria Tracking in Microfluidic Channels

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The bacterial suspensions are visualized using an inverted microscope (Zeiss Observer, Z1), with an air objective (63×/0.75 LD Plan) and equipped with a Hamamatsu camera (ORCA-Flash 4.0, C11440) at a frame rate of 200 frames per second (fps) at 1024 × 512 pixels (typical field-of-view size of 200 μm by 100 μm). Using a high frame rate is important to track bacteria at high flow rates since bacteria displacements in between two frames need to be small compared to a typical distance between two adjacent bacteria. Because of the use of an air lens, there is a mismatch of refraction index with the solution in the channel and height measurements need to be corrected by a factor of 1.3622. Two methods are used to control the local shear rates in the channel: varying the flow rate Q at a given distance from the bottom wall (z = 0.1H and z = 0.2H), called Q scan, and gradually increasing the distance from the bottom wall with steps δz = 5 × 1.3622 ≈ 6.8 μm at the given flow rates Q = 5, 10, and 20 nl/s, called z scan. For each position at a given flow rate, 2000 frames are taken as one stack video for the following tracking process. The fluorescent intensity of the RP437 strain is sufficient to allow for a small exposure time of 3 ms.

Jing G., Zöttl A., Clément É, & Lindner A. (2020). Chirality-induced bacterial rheotaxis in bulk shear flows. Science Advances, 6(28), eabb2012.

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Wide-field Fluorescence Microscopy Imaging

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Imaging experiments were performed on a Nikon Ti-Eclipse inverted wide-field epifluorescence deconvolution microscope (Nikon Corporation). Images were collected using an Orca-Flash 4.0 C11440 (Hamamatsu Photonics) camera and Nikon NIS Elements software (version 4.20.03) using Nikon 4x/0.13 (Plan Apo) objective lense and the following excitation/emission filter set ranges (wavelengths in nanometers): 418-442/458-482 (CFP), 490-510/520-550 (YFP), and 555-589/602-662 (mCherry).

Knoener R., Evans E I.I.I., Becker J.T., Scalf M., Benner B., Sherer N.M, & Smith L.M. (2021). Identification of host proteins differentially associated with HIV-1 RNA splice variants. eLife, 10, e62470.

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Multimodal Microscopy Imaging Workflow

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For phase contrast and darkfield imaging, an Olympus ix83 inverted microscope with LUCPlanFLNPh 20× objective and a phase contrast plate were used. The condenser of the microscope was retrofitted with an oblique angle LED ring illuminator (Amscope LED-144-YK ring lamp) to allow for darkfield imaging. A Hamamatsu Orca Flash 4.0 C11440 at a 16-bit depth with a 0.16–0.33 μm pixel resolution were used to record images. Tile scans and image stitching were performed using the MetaMorph Premier (64-bit) 7.8.12.0 software. Details on image processing and data analysis can be found in the Supplementary Information.

Touloumes G.J., Ardoña H.A., Casalino E.K., Zimmerman J.F., Chantre C.O., Bitounis D., Demokritou P, & Parker K.K. (2020). Mapping 2D- and 3D-distributions of metal/metal oxide nanoparticles within cleared human ex vivo skin tissues. NanoImpact, 17, 100208.

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Exocytosis Visualization of tPA-GFP Granules

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The optical instrument for visualizing the exocytosis process of tPA‐GFP secretory granules consisted of an Olympus inverted microscope (IX81; Olympus Corp., Tokyo, Japan, 60×/1.45 numeric aperture oil‐immersion objective) equipped with a TIRF unit for generating an evanescent field which enabled us to excite only the fluorophore present in the immediate vicinity of the plasma membrane; an automatic focus device (ZDC2); a digital complementary metal oxide semiconductor (CMOS) camera (ORCA‐Flash4.0, C11440; Hamamatsu Photonics, Hamamatsu, Japan), and a temperature controller to keep the cells at 37 °C on the microscope stage (INUG2‐ONID‐BE; Tokai Hit, Shizuoka, Japan). tPAs‐GFP was excited by a 488‐nm laser with a 1.3 neutral density filter (Edmond Optics, Tokyo, Japan), and emissions were collected through a 520/35‐nm band pass filter (Semrock, Rochester, NY, USA). HCImage software (Hamamatsu Photonics) was used to capture the fluorescence images. The fluorescence intensity of an ROI in individual secretory granules was measured and analyzed on an Aquacosmos imaging station (Hamamatsu Photonics).

Suzuki Y., Sano H., Tomczyk M., Brzoska T, & Urano T. (2016). Activities of wild‐type and variant tissue‐type plasminogen activators retained on vascular endothelial cells. FEBS Open Bio, 6(5), 469-476.

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Bioadhesive Fiber Scaffold Characterization

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To evaluate the bioadhesive property of the fiber scaffolds, we assessed the extent of fibronectin (FN, BD Biosciences, CA, USA) coating at the fiber surfaces. The spun fiber scaffolds were incubated with 50 μg/mL of FN solution in deionized water for 6 h at room temperature. After which, the samples were washed with deionized water 3 times and were then incubated with anti-FN antibody (rabbit, Abcam, MA, USA) and a secondary antibody (goat anti-rabbit IgG (H+L) conjugated with Alexa Fluor® 546, Invitrogen, Thermo Fischer Scientific, MA, USA) separately, for 1 h each. The micrographs of the fluorescently stained samples were obtained using a spinning disk confocal microscope (Olympus ix83, Andor spinning disk). The images were recorded on a Hamamatsu Orca Flash 4.0 C11440 at 16-bit depth with a 0.16 μm to 0.33 μm pixel resolution. For the statistical analysis of FN absorption on the nanofiber, the fluorescent FN images on the nanofiber were recorded for multiple samples (n=3) with multiple regions of interest (ROIs, at least 25) for each condition. The coverage of FN on the nanofiber was calculated using ImageJ software and then normalized to the FN coverage on PCL/DA nanofiber using OriginPro 8.6 software.

Ahn S., Ardoña H.A., Lind J.U., Eweje F., Kim S.L., Gonzalez G.M., Liu Q., Zimmerman J.F., Pyrgiotakis G., Zhang Z., Beltran-Huarac J., Carpinone P., Moudgil B.M., Demokritou P, & Parker K.K. (2018). Mussel-inspired 3D Fiber Scaffolds for Heart-on-a-Chip Toxicity Studies of Engineered Nanomaterials. Analytical and bioanalytical chemistry, 410(24), 6141-6154.

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Quantitative DAPI-based cell imaging

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Fixed cells were permeabilized using 0.2% Triton X-100, and stained with DAPI (4′,6′-diamidino-2-phenylindole 4′,6-diamidino-2-phenylindole). DAPI fluorescence was measured using a Cytation 5 Imaging Reader (Biotek Instruments, Inc.) operated by Gen5 software (v 2.07) using excitation/emission monochromator range (wavelengths in nanometers) 340 to 380/420 to 480 (DAPI). Cell number based on the relative DAPI signal is later used to normalize imaging data. Additional imaging experiments were performed on a Nikon Ti-Eclipse inverted wide-field epifluorescent deconvolution microscope (Nikon Corporation). Images were collected using an Orca-Flash 4.0 C11440 (Hamamatsu Photonics) camera and Nikon NIS Elements software (v 4.20.03) using Nikon 4x/0.13 (Plan Apo) objective lense and the following excitation/emission filter set ranges (wavelengths in nanometers): 418 to 442/458 to 482 (CFP), 490 to 510/520 to 550 (YFP), 555 to 589/602 to 662 (mCherry). Images were processed and analyzed using FIJI/ImageJ2^{89 (link)}. Results were obtained from two biological replicates, defined as cells treated with siRNAs and infected with virus on separate days.

Knoener R.A., Becker J.T., Scalf M., Sherer N.M, & Smith L.M. (2017). Elucidating the in vivo interactome of HIV-1 RNA by hybridization capture and mass spectrometry. Scientific Reports, 7, 16965.

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Single-cell Imaging and Fluorescence Analysis

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Single-cell imaging experiments were performed on a Nikon Ti-Eclipse inverted wide-field epifluorescence deconvolution microscope (Nikon Corporation). Images were collected using an Orca-Flash 4.0 C11440 (Hamamatsu Photonics) camera and Nikon NIS Elements software (version 4.20.03) using Nikon 60x (N.A. 1.40; Plan Apo) or 100× (N.A. 1.45; Plan Apo) objective lenses and the following excitation/emission filter set ranges (wavelengths in nanometers): 405/470 (DAPI), 430/470 (CFP), 490/525 (AlexaFluor488), 585/610 (CAL Fluor Red 590), 645/705 (AlexaFluor647). Images were generally acquired in z-stacks containing various numbers of images along the z-axis of the cells. Images were processed and analyzed using FIJI/ImageJ2 (Rueden et al., 2017 (link)). All z-frames within a z-stack were examined for instances of co-localization; however, the fluorescence from only a single z-frame was used to produce co-localization images. For determining HIV RNA, Gag, and host protein expression differences in cells, four z-frames were merged additively for fluorescence quantitation of each component.

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Plasmonic Imaging Microscopy Setup

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The plasmonic imaging setup was built on an inverted total internal reflection microscope (ECLIPSE Ti-E Series, Nikon Instruments Inc.) equipped with a high numerical aperture (NA = 1.49) oil-emersion objective (60×). A beam of p-polarized light from a 680 nm superluminescent diode (SUPERLUM, Ireland) was directed onto the gold film mounted on the objective to excite surface plasmon polaritons, and the reflected light was collected with the same objective and directed to an sCMOS (ORCA-Flash4.0 C11440, Hamamatsu Photonics K.K.), or CCD camera (Pike F-032B, Allied Vision Technologies GmbH) for imaging. The gold chips were prepared by evaporating 2 nm chromium as an adhesion layer followed by a 47 nm gold layer on BK-7 glass coverslips. The gold films were immersed in 10 mM 1-octadecanethiol dissolved in ethanol for 48 h, rinsed with ethanol and water sequentially, and dried with nitrogen gas prior to use.

Zhao X., Zhou X.L., Yang S.Y., Min Y., Chen J.J, & Liu X.W. (2022). Plasmonic imaging of the layer-dependent electrocatalytic activity of two-dimensional catalysts. Nature Communications, 13, 7869.

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Immunostaining Cardiac Muscle Cells

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MTFs were fixed with 4% paraformaldehyde and 0.25% Triton X-100. NRVM's tissues were stained with monoclonal mouse anti-(sarcomeric α-actinin) primary antibody (Sigma), DAPI (Sigma), and phalloidin conjugated to Alexa-Fluor 488 (Invitrogen). Samples were then imaged using Olympus IX-83 spinning disk confocal microscope (Olympus) and recorded on an Orca Flash 4.0 C11440 (Hamamatsu) camera at 16-bit depth, with a 0.16 to 0.33 μm pixel resolution.

Vurro V., Shani K., Ardoña H.A., Zimmerman J.F., Sesti V., Lee K.Y., Jin Q., Bertarelli C., Parker K.K, & Lanzani G. (2023). Light-triggered cardiac microphysiological model. APL Bioengineering, 7(2), 026108.

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