Titan krios

Manufactured by Thermo Fisher Scientific

Sourced in United States, United Kingdom, Netherlands, Germany, China, Sweden

The Titan Krios is a high-performance transmission electron microscope (TEM) designed for cryo-electron microscopy (cryo-EM) applications. It provides high-resolution imaging and data acquisition capabilities for the study of biological macromolecular structures.

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Lab products found in correlation

Vitrobot mark 4, by Thermo Fisher Scientific (259 mentions) K2 summit, by Ametek (47 mentions) Vitrobot, by Thermo Fisher Scientific (47 mentions) Epu software, by Thermo Fisher Scientific (31 mentions) Talos arctica, by Thermo Fisher Scientific (27 mentions) K3 direct electron detector, by Ametek (24 mentions) K3 detector, by Ametek (24 mentions) K2 summit direct electron detector, by Ametek (22 mentions) Mark 4, by Thermo Fisher Scientific (19 mentions) R1.2 1 3 400 mesh au holey carbon grids, by Quantifoil (16 mentions) Em gp2 plunge freezer, by Leica (15 mentions) K3 camera, by Ametek (13 mentions) Gif quantum energy filter, by Ametek (12 mentions) Fei vitrobot mark 4, by Thermo Fisher Scientific (12 mentions) K2 summit detector, by Ametek (11 mentions) Au r1 2 1, by Quantifoil (9 mentions) Bioquantum energy filter, by Ametek (9 mentions) K3 summit, by Ametek (8 mentions) K3 summit direct electron detector, by Ametek (7 mentions) K2 summit, by Thermo Fisher Scientific (7 mentions)

Close spelling variants of this product

FEI Titan Krios microscope (25 citations) FEI Titan Krios electron microscope (17 citations) Titan Krios G4 (15 citations) 300 kV Titan Krios (9 citations) Titan Krios G2 transmission electron microscope (6 citations) Titan Krios G3i TEM (5 citations) Titan Krios transmission electron (5 citations) Titan Krios (300KV) electron microscope (5 citations) TFS Titan Krios (5 citations) 300 kV TEM Titan Krios (5 citations)

617 protocols using titan krios

Cryo-EM Analysis of SidH Proteins

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For the SidH FL, cryo-EM movies were collected on a Titan Krios (FEI) electron microscope equipped with a K2 Summit direct electron detector and a GIF Quantum energy filter (Gatan) at the EMBL Heidelberg cryo-EM platform. The operational acceleration voltage for the microscope was 300 kV. The defocus values ranged from −0.8 to −2.0 μm. The dose rate on the camera was set to be about 3 e⁻/pixel/second in electron counting mode. The total exposure time for each movie was 8 s with a total exposure dose of 41.93 e/ Å² on the sample. Each movie was fractionated into 40 frames, with 0.2 s per frame. 9020 images were collected with a pixel size of 0.81 Å.
For SidH_LubX complex, 9195 images were collected with a pixel size of 0.827 Å on Titan Krios (FEI) electron microscope at the ESRF Grenoble cryo-EM platform CM01 equipped with K2 direct electron detector^{39 (link)}. The images were collected in electron counting mode with a dose rate of about 7 e⁻/pixel/second. The total exposure time for each movie was 4 s with a total exposure dose of 43.37 e/ Å² on the sample. Each movie was fractionated into 40 frames, with 0.1 s per frame.

Sharma R., Adams M., Griffith-Jones S., Sahr T., Gomez-Valero L., Weis F., Hons M., Gharbi S., Berkane R., Stolz A., Buchrieser C, & Bhogaraju S. (2023). Structural basis for the toxicity of Legionella pneumophila effector SidH. Nature Communications, 14, 7068.

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Cryogenic Imaging of Bacterial Ribosomes

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Elutions from HflX and HflXr pull-downs were kept on ice and applied to grids within 2 h of preparation. 3.5 μl of sample was loaded onto glow discharged cryo-grids (Quantifoil 2/2 Cu300 coated with 2 nm continuous carbon) using the Vitrobot (FEI) under conditions of 100% humidity at 4°C, blotted for 5 s and vitrified by plunge-freezing in liquid ethane. HflXr samples were imaged on a Titan Krios (FEI) operated at 300 kV at a nominal magnification of ×165,000 (0.86 Å/pixel) with a Gatan K2 Summit camera. HflXr-50S samples were imaged at an exposure rate of 5.85 electrons/pixel/s with a 4 s of exposure and 20 frames using the EPU software. HflX-50S samples were imaged at the exposure rate of 6.899 electrons/pixel/s with a 3.2 s of exposure.
Purified 70S L. monocytogenes ribosomes at a concentration of 0.4 μM were incubated with 100 μM lincomycin on ice before 4 μl of sample was loaded onto glow discharged cryo-grids (Quantifoil 2/2 Cu300 coated with 2 nm continuous carbon) using the Vitrobot (FEI) as described above. Data was collected on a Titan Krios (FEI) operated at 300 kV at a nominal magnification of ×270,000 (0.502 Å/pixel) with a Gatan K2 Summit camera at an exposure rate of 3.38 electrons/pixel/s with a 3 s of exposure and 20 frames using the EPU software.

Koller T.O., Turnbull K.J., Vaitkevicius K., Crowe-McAuliffe C., Roghanian M., Bulvas O., Nakamoto J.A., Kurata T., Julius C., Atkinson G.C., Johansson J., Hauryliuk V, & Wilson D.N. (2022). Structural basis for HflXr-mediated antibiotic resistance in Listeria monocytogenes. Nucleic Acids Research, 50(19), 11285-11300.

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Cryo-EM Imaging of IGF2R Complexes

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Freshly purified apo state IGF2R (4 to 5 mg/ml) in buffer A and the IGF2R-IGF2 complex (4 to 5 mg/ml) in buffer B were added to Quantifoil R1.2/1.3 400 mesh Au holey carbon grids (Quantifoil), blotted using a Vitrobot Mark IV (FEI), and frozen in liquid ethane. The grid of the apo state IGF2R protein was imaged using a 300-keV Titan Krios (FEI) with a Gatan K2 Summit direct electron detector (Gatan). The data were collected in superresolution mode at a pixel size of 0.5 Å with a dose rate of ~2 electrons per pixel per second. Images were recorded for 10-s exposures in 50 subframes to give a total dose of ~80 electrons/Å². The grid of the IGF2-IGF2R complex was imaged using a 300-keV Titan Krios (FEI) with a Gatan K3 Summit direct electron detector (Gatan). The data were collected in superresolution mode at a pixel size of 0.43 Å with a dose rate of ~6 electrons per pixel per second. Images were recorded for 3-s exposures in 75 subframes to give a total dose of ~100 electrons/Å². The grid of ligand-free IGF2R was imaged using a 200-keV Talos Arctica (FEI) with a Gatan K3 Summit direct electron detector (Gatan). The data were collected in superresolution mode at a pixel size of 0.445 Å with a dose rate of ~6 electrons per pixel per second. Images were recorded for 2-s exposures in 40 subframes to give a total dose of ~60 electrons/Å².

Wang R., Qi X., Schmiege P., Coutavas E, & Li X. (2020). Marked structural rearrangement of mannose 6-phosphate/IGF2 receptor at different pH environments. Science Advances, 6(7), eaaz1466.

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Cryo-EM Imaging of Beta Proteins

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Compressed tif format movies were acquired on a Titan Krios (Thermo Fisher) operating at 300 kV with a K2 detector with 20 eV slit (Gatan) at a nominal magnification of 165 kX (corresponding to a calibrated pixel size of 0.82 Å/pix) and defocus range of 0.8-2.6 μm. For Beta-26, Beta-32, Beta-43, Beta-49, Beta-50 and Beta-53, movies were acquired also on a Titan Krios (Thermo Fisher) as for Beta-6 except with a 10 eV slit and 70 μm C2 aperture.

Liu C., Zhou D., Nutalai R., Duyvesteyn H.M., Tuekprakhon A., Ginn H.M., Dejnirattisai W., Supasa P., Mentzer A.J., Wang B., Case J.B., Zhao Y., Skelly D.T., Chen R.E., Johnson S.A., Ritter T.G., Mason C., Malik T., Temperton N., Paterson N.G., Williams M.A., Hall D.R., Clare D.K., Howe A., Goulder P.J., Fry E.E., Diamond M.S., Mongkolsapaya J., Ren J., Stuart D.I, & Screaton G.R. (2022). The antibody response to SARS-CoV-2 Beta underscores the antigenic distance to other variants. Cell Host & Microbe, 30(1), 53-68.e12.

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Cryo-EM Structural Analysis of LASV Glycoprotein

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Purified LI-LASV-pfGP-25.10C complexes were concentrated to 0.7 mg/mL, and a 3-μL aliquot was mixed with 1 μL 0.02 mM lauryl maltose neopentyl glycol (LMNG) detergent. No detergent was added to the LI-pfGP-18.5C-M30 complex. The samples (3 μL) were applied to C-flat 2/1 copper grids that had been plasma cleaned for 30 s in a NanoClean model 1070 (Fischione Instruments) using a mixture of 25% oxygen and 75% argon. Grids were blotted for 10 s to remove excess solution and then plunge-frozen in liquid ethane using an FEI Vitrobot (Thermo Fisher Scientific). Frozen grids containing LI-pfGP-25.10C were imaged using a Titan Krios (Thermo Fisher Scientific) equipped with a Gatan K2 detector, while grids containing LI-pfGP-18.5C-M30 were imaged using a Titan Krios equipped with a Gatan K3 detector. Movies for the LI-pfGP-25.10C complex were collected at a magnification of ×46,300 in super resolution mode and correspond to a calibrated pixel size of 0.548 Å/pixel. Movies were collected in a single session with a defocus range between 1.0 and 2.5 μm underfocus. Movies for the LI-pfGP-18.5C-M30 complex were collected at a magnification of ×75,750 in counting mode that corresponds to a calibrated pixel size of 0.6656. A full description of the cryo-EM data collection parameters is presented in Tables S1 and S2 in the supplemental material.

Buck T.K., Enriquez A.S., Schendel S.L., Zandonatti M.A., Harkins S.S., Li H., Moon-Walker A., Robinson J.E., Branco L.M., Garry R.F., Saphire E.O, & Hastie K.M. (2022). Neutralizing Antibodies against Lassa Virus Lineage I. mBio, 13(4), e01278-22.

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Cryo-EM Imaging of Bacteriophages

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Data were collected on a 300 keV Titan Krios (Thermo Fisher Scientific, Waltham, Massachusetts, USA) at the Pacific Northwest Center for Cryo-EM with either a K3 or Falcon 3 direct electron detector (Gatan, Pleasanton, CA, USA). The data for Muddy was collected on a 300 keV Titan Krios 3Gi at the University of Pittsburgh with a Falcon 3 direct electron detector (Thermo Fisher Scientific, Waltham, Massachusetts, USA). Table S1 provides the collection parameters for each phage.

Podgorski J.M., Freeman K., Gosselin S., Huet A., Conway J.F., Bird M., Grecco J., Patel S., Jacobs-Sera D., Hatfull G., Gogarten J.P., Ravantti J, & White S.J. (2023). A structural dendrogram of the actinobacteriophage major capsid proteins provides important structural insights into the evolution of capsid stability. Structure (London, England : 1993), 31(3), 282-294.e5.

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Cryo-EM Structure Determination of CPLANE

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Data were collected automatically with EPU (Thermo Fisher Scientific) on a Cs-corrected (CEOS GmbH, Heidelberg, Germany) Titan Krios (Thermo Fisher Scientific) electron microscope at 300 keV. Four sessions for a total of 13,056 zero-energy loss movies of the mouse CPLANE complex were recorded using a Gatan K2 summit direct electron detector (Gatan) operating in counting mode and located after a Quantum-LS energy filter (slit width of 20 eV). The acquisition was performed at a magnification of 130,000× yielding a pixel size of 0.86 Å at the specimen level. Datasets were recorded with dose rates between 3.5 and 5 e⁻/(px·s), and the exposures were fractionated into 50 frames for an accumulated dose of 52 e⁻/Å². The targeted defocus values ranged from −0.8 to −2.5 μm. The data for the human CPLANE complex (5619 movies) were collected on the same Titan Krios but using a Falcon 4 (Thermo Fisher Scientific) instead. The magnification was 96,000× with a pixel size of 0.66 Å. The dose rate was set to 18.3 e⁻/Å/s, and the exposure time was adjusted to account for an accumulated dose of 50 e⁻/Å². The EER frames were grouped to obtain 50 fractions.

Langousis G., Cavadini S., Boegholm N., Lorentzen E., Kempf G, & Matthias P. (2022). Structure of the ciliogenesis-associated CPLANE complex. Science Advances, 8(15), eabn0832.

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Cryo-EM Visualization of Tau Filaments

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Samples were applied to glow-discharged holey carbon gold grids (Quantifoil R1.2/1.3, 300 mesh), and plunge frozen in liquid ethane using an FEI Vitrobot Mark IV. Images of the samples from the AD case used Gatan K2 summit and K3 detectors in counting mode on a Titan Krios (Thermo Fisher) at 300 kV for +flortaucipir and -flortaucipir samples respectively. A GIF quantum energy filter (Gatan) was used with a slit width of 20 eV to remove inelastically scattered electrons. Images of the samples from the PART case were acquired using a Falcon-4 detector without energy filter in counting mode on a Titan Krios (Thermo Fisher) at 300 kV. Further details are given in Supplementary Table 1. To increase the accessibility of flortaucipir to the core of tau filaments, samples (with and without flortaucipir) of the case with PART were treated with 0.1 mg/ml of pronase for 30–40 min, prior to making grids.^{45 (link)}

Shi Y., Ghetti B., Goedert M, & Scheres S.H. (2023). Cryo-EM Structures of Chronic Traumatic Encephalopathy Tau Filaments with PET Ligand Flortaucipir. Journal of molecular biology, 435(11), 168025.

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Cryo-EM Structure Determination of NaV Channel

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Cryo-EM grids were prepared by applying freshly purified MBP-disulfide locked resting state Na_VAb in digitonin detergent to glow-discharged holey carbon grids (C-Flat Cu R1.2/1.3, EMS). Grids were manually blotted for 4 to 5 s and immediately plunge-frozen in liquid ethane cooled by liquid nitrogen. Cryo-EM data were recorded on a Titan Krios (FEI) operated at 300 kV, equipped with a GIF-quantum energy filter (Gatan) at 20 eV slit width and a K2 Summit direct detector (Gatan). LEGINON (Suloway et al., 2005 (link)) was used for automated data collection. Movies were collected at a nominal magnification of 130,000x in super-resolution mode resulting in a pixel size of 0.528 Å, with a small defocus range of –0.5 to –2.5 μm. The dose rate on the camera was set to be ~8 counts per physical pixel per second. The total exposure time was 8.6 s (0.2 s/frame), leading to a total accumulate dose of 60 electrons per Å² on the specimen (Table S2).

Wisedchaisri G., Tonggu L., McCord E., Gamal El-Din T.M., Wang L., Zheng N, & Catterall W.A. (2019). Resting State Structure and Gating Mechanism of a Voltage-gated Sodium Channel. Cell, 178(4), 993-1003.e12.

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Structural Studies of PORCN-Ligand Complexes

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PORCN samples (~8 mg/ml) with 10 μM LGK974 and HHAT–SHH-N–Fab^3H02 complex (~10mg/ml) were applied to Quantifoil R1.2/1.3 400 mesh Au holey carbon grids (Quantifoil), respectively. For the preparation of palmitoleoyl-CoA-bound PORCN samples, palmitoleoyl-CoA was added into the apo-PORCN sample at the final concentration of 1 mM before vitrification. For the preparation of LGK974/WNT3Ap-bound PORCN samples, WNT3Ap (MHLKCKCHGLSGSCEVKTCWWS, C5-C19, C7-C14, Biomatik) were mixed with LGK974-bound PORCN at a final concentration of 1 mM. For the preparation of product-bound PORCN, pamWNT3Ap was added into the apo-PORCN at the final concentration of 1.2 mM. The above two peptide mixtures were incubated on ice for 30 min before vitrification. The grids were blotted and plunged into liquid ethane for flash freezing using a Vitrobot Mark IV (FEI). The grids were imaged in a 300 kV Titan Krios (FEI) with a Gatan K3 Summit direct electron detector (Gatan). Data were collected using SerialEM ^{45 (link)} at 0.83 Å/pixel or 0.842 Å/pixel. Images were recorded for 5-second exposures in 50 subframes with a total dose of ~60 electrons per Å².

Liu Y., Qi X., Donnelly L., Elghobashi-Meinhardt N., Long T., Zhou R.W., Sun Y., Wang B, & Li X. (2022). Mechanisms and Inhibition of Porcupine-Mediated Wnt Acylation. Nature, 607(7920), 816-822.

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