Titan krios cryo electron microscope

Manufactured by Ametek

The Titan Krios cryo-electron microscope is a high-performance instrument designed for advanced cryo-electron microscopy applications. It features a stable and powerful electron beam, advanced imaging capabilities, and a cryogenic specimen stage for maintaining samples in a frozen state. The Titan Krios is a versatile tool that enables researchers to study the structure and function of biological macromolecules at high resolution.

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Lab products found in correlation

K2 camera, by Ametek (2 mentions) 4k x 4k ccd, by Ametek (2 mentions) Vitrobot, by Thermo Fisher Scientific (2 mentions) K3 direct electron counting camera, by Ametek (1 mentions) Ultraufoil r1 2 1, by Quantifoil (1 mentions) Titan krios cryo electron microscope, by Thermo Fisher Scientific (1 mentions) K2 summit camera, by Ametek (1 mentions) K2 summit, by Ametek (1 mentions)

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5 protocols using titan krios cryo electron microscope

Cryo-EM Structure of Lb2Cas12a Ribonucleoprotein

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Purified Lb2Cas12a, crRNA with 20 nt guide sequences, and DNA were mixed in a ratio of 1:1.5:2 and remove excess nucleic acid by gel filtration chromatography. The fresh sample was purified at 0.5 mg/ml in buffer containing 20 mM HEPES-Na (pH 7), 150 mM NaCl, 10 mM MgCl₂, 5 mM DTT. The cryo-EM data were collected at CBIS CryoEM Facility, National University of Singapore. Four microliters of sample were applied on glow-discharged UltrAufoil R1.2/1.3 (Quantifoil) and blotted for 1 s in 22°C with 100% humidity, a wait time of 15 s, a drain time of 0 s, and a force of −5 using FEI Vitrobot Marc IV. The grid was plunge-frozen in liquid ethane cooled by liquid nitrogen. The frozen-hydrated grid was loaded into Titan Krios cryo-electron microscope equipped with Gatan K3 direct-electron counting camera and operated at 300 keV, and 35-frame movies were collected at 81,000× magnification in counting mode with a physical pixel size of 1.105 Å/pixel. The images were recorded at defocus range of 0.5 to 2.5 μm. The exposure time was 3.49 s. The dose was 45 e/Å per movie stack. The 2,560 stacks of 35-frame movies were collected, using SerialEM program (FEI; Thermo Fisher Scientific).

Jianwei L., Jobichen C., Machida S., Meng S., Read R.J., Hongying C., Jian S., Yuan Y.A, & Sivaraman J. (2023). Structures of apo Cas12a and its complex with crRNA and DNA reveal the dynamics of ternary complex formation and target DNA cleavage. PLOS Biology, 21(3), e3002023.

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Cryo-EM Structural Analysis of Resting and Desensitized Ion Channels

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For the resting channel structure at high pH, data were collected on a Titan Krios cryo-electron microscope (ThermoFisher) operated at 300 keV. Images were recorded on a Gatan K3 camera positioned after an energy filter (20 eV slit width) operating in super-resolution mode with a binned pixel size of 0.648 Å. Data were collected with SerialEM (Mastronarde, 2003 (link)) and dose-fractionated to 50 frames for a total exposure time of 2–3 s and a total dose of 40–50 e^- Å⁻².
For the desensitized state structure at pH 7.0, data were recorded on a Titan Krios cryo-electron microscope operated at 300 kV and equipped with a spherical aberration corrector. Images were recorded on a Gatan K2 Summit camera in super-resolution mode with a binned pixel size of 1.096 Å. Data were acquired using Leginon (Suloway et al., 2005 (link)) and dose-fractionated to 48 frames at 0.15 s per frame for a total exposure time of 7.25 s and a total dose of 50 e^- Å⁻².

Yoder N, & Gouaux E. (2020). The His-Gly motif of acid-sensing ion channels resides in a reentrant ‘loop’ implicated in gating and ion selectivity. eLife, 9, e56527.

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Cryogenic Electron Microscopy of Bluetongue Virus

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Virions were purified as described^{18 (link)}. To prepare cryoEM grids, 2μl purified BTV sample (pH8.8) was applied to thin continuous carbon films. After 3 minutes, the sample was blotted, and 2μl citrate buffer (pH3.4 or 5.5) was immediately applied to the grid for 30 seconds. The grid was blotted for 9 seconds in an FEI Vitrobot with 100% humidity and then plunged into liquid ethane. CryoEM images were collected in an FEI Titan Krios cryo electron microscope operated at 300kV. For the pH3.4 condition, a total of 350 images were recorded on a Gatan 4k x 4k CCD at a calibrated magnification of 79,370x, corresponding to a pixel size of 1.89Å/pix on the specimen. A total of 7474 particles were selected for data processing as described above, and the final 3D map was reconstructed from 4503 particles at a resolution of 9.0Å (FSC=0.143). For the pH5.5 condition, 159 particle images recorded on a Gatan K2 camera were used for a reconstruction at 25Å resolution (FSC=0.143), which appears identical to that of the above pH3.4 structure filtered to the same resolution.

Zhang X., Patel A., Celma C.C., Yu X., Roy P, & Zhou Z.H. (2015). Atomic model of a non-enveloped virus reveals pH sensors for a coordinated process of cell entry. Nature structural & molecular biology, 23(1), 74-80.

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Cryogenic Electron Microscopy of Bluetongue Virus

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Cryogenic Imaging of Sparse Viral Particles

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Aliquots of 2.5 μl of the sample were applied to 200-mesh Quantifoil R2/1 cooper grids, blotted with filter paper and plunge-frozen into liquid ethane with a manual plunger. These grids were stored in a liquid nitrogen Dewar before cryo-EM imaging. Cryo-EM was performed in an FEI Titan Krios cryo-electron microscope equipped with a Gatan imaging filter (GIF) and a post-GIF Gatan K2 Summit direct electron detector. Before imaging, the electron microscope was carefully aligned and the parallel beam was optimized using the coma-free alignment tool in SerialEM40. The microscope was operated at 300 kV with the GIF slit set to 20 eV. Movies were recorded at a dose rate of ~8.5 electrons per s per physical pixel on the detector with a ×105,000 nominal magnification (corresponding to a pixel size of 0.68 Å at the specimen level) in super-resolution mode. The total exposure time for each movie was 6 s, fractionated equally into 30 frames, leading to a total dosage of ~28 electrons Å⁻² on the specimen. We circumvented the scarcity of virion particles by employing a combination of advanced imaging technologies^{40 (link)–42 (link)} to precisely target sparsely distributed EBV virions (barely one particle per movie, for example, see Supplementary Fig. 1). A total of 3,908 movies were recorded in a continued session spanning 3 d.

Liu W., Cui Y., Wang C., Li Z., Gong D., Dai X., Bi G.Q., Sun R, & Zhou Z.H. (2020). Structures of capsid and capsid-associated tegument complex inside the Epstein–Barr virus. Nature microbiology, 5(10), 1285-1298.

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