Temcam f416 cmos camera

Manufactured by TVIPS

Sourced in Germany

The TemCam-F416 CMOS camera is a high-performance imaging device designed for use in electron microscopy applications. The camera features a 4096 x 4096 pixel sensor, enabling the capture of high-resolution images. The camera is capable of operating at a maximum frame rate of 16 frames per second, making it suitable for a variety of imaging tasks. The camera's design and functionality are intended to provide users with a reliable and efficient imaging solution for their research and analysis needs.

Automatically generated - may contain errors

Lab products found in correlation

21 protocols using temcam f416 cmos camera

Proteoliposome Reconstitution and Imaging

Check if the same lab product or an alternative is used in the 5 most similar protocols

Proteoliposomes reconstituted with autophagic SNARE proteins at an L/P ratio of 800 were incubated with or without Atg14 (54 nM) at 37 °C for 3 h. Samples were centrifuged at 800g. for 2 min to remove large aggregations. Frozen-hydrated samples were prepared using the procedures described previously^{18 (link)}. Samples were imaged in low-dose conditions using a TF20 electron microscope (FEI) operating at 200 kV. Images of both conditions were collected at a nominal magnification of ×29,000 and an under-focus of 2.5–3.5 μm on a TemCam-F416 CMOS camera (TVIPS GmbH, 4,096 pixels ×4,096 pixels). Bar graphs of the percentage of hemifused or clustered proteoliposomes (Fig. 2g) were obtained by visual inspection of 20 micrographs, using 1,079 and 661 observed proteoliposomes without and with ATG14, respectively.

Diao J., Liu R., Rong Y., Zhao M., Zhang J., Lai Y., Zhou Q., Wilz L.M., Li J., Vivona S., Pfuetzner R.A., Brunger A.T, & Zhong Q. (2015). ATG14 promotes membrane tethering and fusion of autophagosomes to endolysosomes. Nature, 520(7548), 563-566.

+ Open protocol

+ Expand

Electron Diffraction of Nanocrystals

Cited 2 times

Check if the same lab product or an alternative is used in the 5 most similar protocols

Electron diffraction datasets from separate crystals were collected using an FEI Tecnai F20 transmission electron microscope operated at 200 kV, with the objective aperture fully open to evenly illuminate an area extending beyond the sample and setting the selected area aperture to closely match the size of the crystal. For each crystal of thickness 200–400 nm, the same 23° wedge was repeatedly collected up to five times by continuously rotating the stage from −12° to +11° (−38° to −15° for crystal 3) off its untilted orientation at a constant rate of 0.089° s⁻¹ (Nannenga et al., 2014b (link)). The rate of electron exposure was adjusted to 0.007 e⁻ Å⁻² s⁻¹, calibrated using a Faraday cage. The individual datasets, each consisting of 49–50 frames with exposure time 5.1s were recorded at a camera length setting of 1.2 m, corresponding to an effective detector distance of 2.2 m. All diffraction images were acquired using a TVIPS TemCam-F416 CMOS camera and corrected to account for negative pixel values (Hattne et al., 2015 (link), 2016 (link)) prior to further processing.

Hattne J., Shi D., Glynn C., Zee C.T., Gallagher-Jones M., Martynowycz M.W., Rodriguez J.A, & Gonen T. (2018). Analysis of Global and Site-Specific Radiation Damage in Cryo-EM. Structure (London, England : 1993), 26(5), 759-766.e4.

+ Open protocol

+ Expand

Cryo-TEM Characterization of Microbial Consortium

Check if the same lab product or an alternative is used in the 5 most similar protocols

The consortium was visualized in mid-stationary phase (12 h incubation, MMSY, 0.6 mM SMX) by Cryo-Transmission Electron Microscopy (Cryo-TEM) for morphological characterization. Briefly, a 4 μl aliquot of the overnight grown liquid culture was adsorbed onto a holey carbon-coated grid (Lacey, Tedpella, USA), blotted with Whatman 1 filter paper and vitrified into liquid ethane at − 180 °C using a vitrobot (FEI, USA). Frozen grids were transferred onto a Talos Electron microscope (FEI, USA) using a Gatan 626 cryo-holder (GATAN, USA). Electron micrographs were recorded at an accelerating voltage of 200 kV using a low-dose system (20 to 40 e−/Å2) and keeping the sample at − 175 °C. Defocus values were − 3 to 6 μm. Micrographs were recorded on 4 K × 4 K Ceta CMOS camera. The cell size, and periplasmic and cell wall thickness were measured with Fiji from the ImageJ platform [101 (link)]. For Transmission Electron Microscopy (TEM) analyses, 4 μl aliquot of the sample was adsorbed onto a glow-discharged carbon film-coated copper grid, and subsequently negatively stained with 2% uranyl acetate. Images were recorded using Philips CM200FEG electron microscope operating at 200 kV on TemCam-F416 CMOS camera (TVIPS, Germany).

Reis A.C., Kolvenbach B.A., Chami M., Gales L., Egas C., Corvini P.F, & Nunes O.C. (2019). Comparative genomics reveals a novel genetic organization of the sad cluster in the sulfonamide-degrader ‘Candidatus Leucobacter sulfamidivorax’ strain GP. BMC Genomics, 20, 885.

+ Open protocol

+ Expand

Transmission Electron Microscope Imaging

Check if the same lab product or an alternative is used in the 5 most similar protocols

Samples were bound to a glow discharged carbon foil covered grid. After staining with 1% uranyl acetate, the samples were evaluated with a CM 120 transmission electron microscope (FEI, Eindhoven, and The Netherlands). Images were taken with a TemCam F416 CMOS camera (TVIPS, Gauting, Germany).

Kolog Gulko M., Heinrich G., Gross C., Popova B., Valerius O., Neumann P., Ficner R, & Braus G.H. (2018). Sem1 links proteasome stability and specificity to multicellular development. PLoS Genetics, 14(2), e1007141.

+ Open protocol

+ Expand

Virus Particle Visualization via ns-TEM

Check if the same lab product or an alternative is used in the 5 most similar protocols

Virus particles released in cell population-derived infections (MOI = 10; 12 hpi) were inactivated using β-propiolactone and then visualized utilizing ns-TEM. The samples were bound to a glow-discharged carbon foil-covered grid and stained using 1% uranyl acetate. Grids were imaged at room temperature using a CM-120 BioTwin transmission electron microscope (Philips). Images were acquired using a TemCam-F416 CMOS camera (TVIPS).

Kupke S.Y., Riedel D., Frensing T., Zmora P, & Reichl U. (2019). A Novel Type of Influenza A Virus-Derived Defective Interfering Particle with Nucleotide Substitutions in Its Genome. Journal of Virology, 93(4), e01786-18.

+ Open protocol

+ Expand

Negative Staining Electron Microscopy

Check if the same lab product or an alternative is used in the 5 most similar protocols

Electron microscopy was performed at the EMBION facility (embion.au.dk), iNANO, Aarhus University. 3 μL of a diluted sample was added to a 400 mesh collodion (Sigma Aldrich) and carbon coated copper grid (Pelco) that had been glow discharged 45s at 25 mA and 39 mbar using an EasiGlow (Pelco). After a 30s incubation, the grid was blotted using a 85 mm filter paper grade 1 (lot. no. 10302, Whatman) and washed/stained 3x with 3 µL 2% uranyl formate (Polysciences Europe GmbH) with blotting steps between each washing/staining step and a final blotting and drying step. Micrographs were collected using a Tecnai Spirit TWIN transmission electron microscope (ThermoFisherScientific) operated at 120 kV using a TemCam F416 CMOS camera and EM-Menu software (Tvips).

Gram H., Theologidis V., Boesen T, & Jensen P.H. (2023). Sarkosyl differentially solubilizes patient-derived alpha-synuclein fibril strains. Frontiers in Molecular Biosciences, 10, 1177556.

+ Open protocol

+ Expand

Transmission Electron Microscopy Sample Preparation

Check if the same lab product or an alternative is used in the 5 most similar protocols

Samples were bound to a glow discharged carbon foil covered copper grid. After washing of the grids using ddH₂O, the samples were stained using 1% uranyl acetate. The samples were evaluated at room temperature using a CM 120 transmission electron microscope (FEI, Eindhoven, and The Netherlands) and a TemCam F416 CMOS camera (TVIPS, Gauting, Germany).

Cabrales Fontela Y., Kadavath H., Biernat J., Riedel D., Mandelkow E, & Zweckstetter M. (2017). Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau. Nature Communications, 8, 1981.

+ Open protocol

+ Expand

Continuous Rotation Electron Diffraction of Lysozyme Microcrystals

Cited 1 time

Check if the same lab product or an alternative is used in the 5 most similar protocols

Lysozyme microcrystals and EM samples for diffraction were prepared as described previously^{4 (link)}. All electron diffraction was performed with intensity less than 0.01 e⁻/Å² on a TEM operated at 200 kV, equipped with an FEG, and data were collected with 4k × 4k TVIPS TemCam-F416 CMOS camera in rolling shutter mode (15.6 μm pixel size). For continuously rotating diffraction data the stage of the microscope was set to rotate at 0.09° s⁻¹ using the microscope’s standard hardware and software. Crystals were located on the grid by searching in over-focused diffraction mode. When a crystal was found, an initial diffraction pattern was recorded to judge the quality of that particular crystal. If the crystal showed strong and sharp diffraction²⁰, the beam was blanked and the rotation of the stage was started. Once the stage began its rotation and had achieved a constant rate, the beam was unblanked and diffraction data were recorded at a constant frame rate of 1 frame per 4 s (0.36°/frame) using the camera’s rolling shutter mode. Data sets of approximately 44° were collected for each crystal (total dose <5e⁻/Å², see supplementary results for dose rate). For the radiation damage assessment, the stage was set at 0° and oscillated back and forth between −1° and 1° during the course of the continuous dosage experiment.

Nannenga B.L., Shi D., Leslie A.G, & Gonen T. (2014). High-resolution structure determination by continuous rotation data collection in MicroED. Nature methods, 11(9), 927-930.

+ Open protocol

+ Expand

Structural Analysis of CV-A21 Virus Particles

Cited 1 time

Check if the same lab product or an alternative is used in the 5 most similar protocols

Samples featuring CV-A21 particles (free or as part of an immune complex) were diluted in TBS to 50 μg/ml and loaded onto in-house made carbon-coated 400-mesh copper grids (glow-discharged at 15 mA for 25 second). The sample was blotted off after 10 seconds and the grids were stained with 2% (w/v) uranyl formate for 60 second. Grids were imaged on a Tecnai F20 electron microscope (FEI) equipped with a TemCam F416 CMOS camera (TVIPS). The microscope operates at 200 kV. The imaging defocus was set to 1.5 µm and the total electron dose adjusted to 25 e⁻/Å². The magnification was set to 62,000×, with the resulting pixel size of 1.77 Å. Leginon software (37 (link)) was used for image acquisition and all the early processing steps were performed in Appion (38 (link)). 2D/3D classification and 3D refinement steps were done in Relion/3.0 (39 (link)). Icosahedral symmetry was imposed for the 3D classification and refinement steps. Negative stain EM maps have been deposited to the EM Data Bank under accession ID EMD-26065.

Antanasijevic A., Schulze A.J., Reddy V.S, & Ward A.B. (2022). High-resolution structural analysis of enterovirus-reactive polyclonal antibodies in complex with whole virions. PNAS Nexus, 1(5), pgac253.

+ Open protocol

+ Expand

Protein Sample Imaging Using TEM

Check if the same lab product or an alternative is used in the 5 most similar protocols

All EM work was done at the iNANO EM facility (EMBION), Aarhus University. Copper grids with a 400 square mesh were prepared with a 2% Collodion solution and carbon coated using a Leica EM SCD 500. The grids were freshly glow-discharged with a PELCO easiGlow™ Glow Discharge Cleaning System prior to loading them with 5 μL of protein sample, blotting and staining 3-times with 3 μL 2% uranyl formate. Samples dilutions 1:5, 1:10, 1:100 and 1:1000 were applied to the grids. TEM images were acquired at a nominal magnification of 67,000× (pixel size size of 1.67 Å) using a FEI Tecnai Spirit transmission electron microscope with a TWIN lens operating at 120 kV. Images were collected with a Tvips TemCam F416 CMOS camera.

Hartmann S., Ling M., Dreyer L.S., Zipori A., Finster K., Grawe S., Jensen L.Z., Borck S., Reicher N., Drace T., Niedermeier D., Jones N.C., Hoffmann S.V., Wex H., Rudich Y., Boesen T, & Šantl-Temkiv T. (2022). Structure and Protein-Protein Interactions of Ice Nucleation Proteins Drive Their Activity. Frontiers in Microbiology, 13, 872306.

+ Open protocol

+ Expand

About PubCompare

Our mission is to provide scientists with the largest repository of trustworthy protocols and intelligent analytical tools, thereby offering them extensive information to design robust protocols aimed at minimizing the risk of failures.

We believe that the most crucial aspect is to grant scientists access to a wide range of reliable sources and new useful tools that surpass human capabilities.

However, we trust in allowing scientists to determine how to construct their own protocols based on this information, as they are the experts in their field.

Ready to get started?

Revolutionizing how scientists
search and build protocols!