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K2 summit detector

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The K2-Summit detector is a high-performance direct electron detector designed for transmission electron microscopy (TEM) applications. It features a large active area, high quantum efficiency, and low noise, enabling high-resolution imaging and data acquisition. The K2-Summit detector is optimized for cryo-electron microscopy (cryo-EM) and other advanced TEM techniques.

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Lab products found in correlation

Vitrobot mark 4, by Thermo Fisher Scientific (12 mentions) Titan krios, by Thermo Fisher Scientific (4 mentions) 300 mesh, by Thermo Fisher Scientific (2 mentions) Au r1 2 1, by Quantifoil (2 mentions) Titan krios g3, by Thermo Fisher Scientific (2 mentions) Titan krios microscope, by Ametek (2 mentions) Vitrobot 4, by Thermo Fisher Scientific (1 mentions) Titan krios microscope, by Thermo Fisher Scientific (1 mentions) K2 summit detector, by Ametek (1 mentions) Talos arctica microscope, by Thermo Fisher Scientific (1 mentions) K3 detector, by Thermo Fisher Scientific (1 mentions) Glacios microscope, by Thermo Fisher Scientific (1 mentions) Tecnai t12 spirit microscope, by Thermo Fisher Scientific (1 mentions) Tecnai f20 microscope, by Thermo Fisher Scientific (1 mentions)

11 protocols using k2 summit detector

1

Cryo-EM Screening of Respiratory and Sperm Axonemes

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Cryo-grids of human respiratory axonemes were screened with either a Tecnai F20 microscope (Thermo Fisher Scientific), equipped with a K2 Summit detector (Gatan), or a Talos Arctica microscope (Thermo Fisher Scientific) equipped with a K3 detector (Gatan) at the Harvard Cryo-EM Center for Structural Biology. Cryo-grids of human sperm samples were screened on a Glacios microscope (Thermo Fisher Scientific) equipped with a K2 Summit detector (Gatan) at the Arnold and Mabel Beckman Cryo-EM Center at the University of Washington. Cryo-grids of animal sperm were screened on an FEI Tecnai Spirit T12 microscope (FEI) at the University of Gothenburg.
Gui M., Croft J.T., Zabeo D., Acharya V., Kollman J.M., Burgoyne T., Höög J.L, & Brown A. (2022). SPACA9 is a lumenal protein of human ciliary singlet and doublet microtubules. Proceedings of the National Academy of Sciences of the United States of America, 119(41), e2207605119.
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2

Cryo-EM of Apaf-1 Apoptosome Assembly

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Three-microliter aliquots of assembled Apaf-1 apoptosome, at a concentration of ∼5 μM, were applied to glow-discharged Quantifoil 400-mesh CuR1.2/1.3 grids. Grids were blotted in a Vitrobot IV (FEI Company) for ∼2–3 sec at 4°C with 100% humidity and then plunge-frozen in liquid ethane. Cryo-EM images of Apaf-1 apoptosome were recorded manually on a K2 Summit detector (Gatan Company) in superresolution mode on an FEI Titan Krios microscope operating at 300 kV. A pixel size of 1.32 Å, defocus values between 1.4 and 3.0 μm, a dose rate of approximately five electrons per square angstrom per second, and an exposure time of 8 sec were used on the K2 Summit detector. UCSFImage4 was used for data collection (developed by Xueming Li).
Zhou M., Li Y., Hu Q., Bai X.C., Huang W., Yan C., Scheres S.H, & Shi Y. (2015). Atomic structure of the apoptosome: mechanism of cytochrome c- and dATP-mediated activation of Apaf-1. Genes & Development, 29(22), 2349-2361.
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3

Cryo-EM Imaging of Tau Filaments

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For cryo-EM, aliquots of 3 μl of purified Tau filaments at a concentration of 1 mg/ml were applied to glow-discharged holey carbon grids (Quantifoil Au R1.2/1.3, 300 mesh), blotted with filter paper to remove excess sample, and plunge-frozen in liquid ethane using an FEI Vitrobot Mark IV. Cryo-EM images were acquired on a Gatan K2-Summit detector in super-resolution counting mode on an FEI Titan Krios at 300 kV. A GIF-Quantum energy filter (Gatan) was used with a slit width of 20 eV to remove inelastically scattered electrons. For full-length filaments (FL), fifty movie frames were recorded each with an exposure time of 200 ms using a dose rate of 1.2 electrons per Å2 per frame for a total accumulated dose of 60 electrons per Å2 at a pixel size of 1.04 Å on the specimen. For pronase-treated filaments (PT), twenty movie frames were recorded, each with an exposure time of 800 ms using a dose rate of 2.75 electrons per Å2 per frame, resulting in a total accumulated dose of 55 electrons per Å2 at a pixel size of 1.15 Å on the specimen. The final data sets are composed of 1560 (FL) and 523 (PT) micrographs with defocus values in both data sets ranging from −1.0 to −3.0 μm.
Fitzpatrick A.W., Falcon B., He S., Murzin A.G., Murshudov G., Garringer H.J., Crowther R.A., Ghetti B., Goedert M, & Scheres S.H. (2017). Cryo-EM structures of Tau filaments from Alzheimer’s disease brain. Nature, 547(7662), 185-190.
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4

Cryo-EM of Pronase-Treated Tau Filaments

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Extracted, pronase-treated tau filaments (3μl at a concentration of ~0.5mg/ml) were applied to glow-discharged holey carbon grids (Quantifoil Au R1.2/1.3, 300 mesh) and plunge-frozen in liquid ethane using an FEI Vitrobot Mark IV. Images were acquired on a Gatan K2-Summit detector in counting mode using an FEI Titan Krios at 300kV. A GIF-quantum energy filter (Gatan) was used with a slit width of 20eV to remove inelastically scattered electrons. Fifty-two movie frames were recorded, each with an exposure time of 250ms using a dose rate of 1.06 electrons per Å2 per frame for a total accumulated dose of 55 electrons per Å2 at a pixel size of 1.15Å on the specimen. Defocus values ranged from −1.7 to −2.8μm. Further details are presented in Exended Data Table 3.
Falcon B., Zhang W., Murzin A.G., Murshudov G., Garringer H.J., Vidal R., Crowther R.A., Ghetti B., Scheres S.H, & Goedert M. (2018). Structures of filaments from Pick’s disease reveal a novel tau protein fold. Nature, 561(7721), 137-140.
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5

Cryogenic Imaging of HIV-1 Envelope

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We applied 3.2 μL PG16(Fab)-gp160 complex (at 0.3 mg/mL) to Quantifoil R 1.2/1.3 holey carbon 200-mesh copper grids (Quantifoil Micro Tools, Großlöbichau, Germany) or (at ~0.015 mg/mL) to C-flat R 1.2./1.3 holey carbon 400 mesh copper grids (Protochips, Morrisville, NC) coated with a thin layer of continuous carbon and plunge-froze in liquid ethane in a Vitrobot Mark 1 (FEI) with 4.2 sec blotting with filter paper pre-saturated at 100% humidity.
We recorded 2510 movies from the samples in open holes, with a K2 Summit detector and a Titan Krios electron microscopy (FEI) automated with SerialEM and operated at 300 kV and nominal magnification of 22,500x (calibrated pixel size 1.31 Å). Those images showed very strong preferential orientation along the gp160 threefold axis, and we therefore also recorded 5628 movies on a K2 Summit detector (Gatan, Inc., Pleasanton, CA) from samples on continuous carbon grids, using a Tecnai Polara electron microscope (FEI) automated with SerialEM [42 (link)] and operated at 300 kV and nominal magnification of 23,000x (calibrated pixel size 1.64 Å). In all cases, we recorded 40 frames/movie in super-resolution mode at a dose rate of 8 electrons/pixel/second and a total exposure of 40 electrons/Å2 (defocus range 1.2–3.0 μm).
Pan J., Peng H., Chen B, & Harrison S.C. (2020). Cryo-EM structure of full-length HIV-1 Env bound with the Fab of antibody PG16. Journal of molecular biology, 432(4), 1158-1168.
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6

Cryo-EM Imaging of Tau Filaments

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For cryo-EM, aliquots of 3 μl of purified Tau filaments at a concentration of 1 mg/ml were applied to glow-discharged holey carbon grids (Quantifoil Au R1.2/1.3, 300 mesh), blotted with filter paper to remove excess sample, and plunge-frozen in liquid ethane using an FEI Vitrobot Mark IV. Cryo-EM images were acquired on a Gatan K2-Summit detector in super-resolution counting mode on an FEI Titan Krios at 300 kV. A GIF-Quantum energy filter (Gatan) was used with a slit width of 20 eV to remove inelastically scattered electrons. For full-length filaments (FL), fifty movie frames were recorded each with an exposure time of 200 ms using a dose rate of 1.2 electrons per Å2 per frame for a total accumulated dose of 60 electrons per Å2 at a pixel size of 1.04 Å on the specimen. For pronase-treated filaments (PT), twenty movie frames were recorded, each with an exposure time of 800 ms using a dose rate of 2.75 electrons per Å2 per frame, resulting in a total accumulated dose of 55 electrons per Å2 at a pixel size of 1.15 Å on the specimen. The final data sets are composed of 1560 (FL) and 523 (PT) micrographs with defocus values in both data sets ranging from −1.0 to −3.0 μm.
Fitzpatrick A.W., Falcon B., He S., Murzin A.G., Murshudov G., Garringer H.J., Crowther R.A., Ghetti B., Goedert M, & Scheres S.H. (2017). Cryo-EM structures of Tau filaments from Alzheimer’s disease brain. Nature, 547(7662), 185-190.
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7

Cryo-EM of Pronase-Treated Tau Filaments

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Extracted, pronase-treated tau filaments (3μl at a concentration of ~0.5mg/ml) were applied to glow-discharged holey carbon grids (Quantifoil Au R1.2/1.3, 300 mesh) and plunge-frozen in liquid ethane using an FEI Vitrobot Mark IV. Images were acquired on a Gatan K2-Summit detector in counting mode using an FEI Titan Krios at 300kV. A GIF-quantum energy filter (Gatan) was used with a slit width of 20eV to remove inelastically scattered electrons. Fifty-two movie frames were recorded, each with an exposure time of 250ms using a dose rate of 1.06 electrons per Å2 per frame for a total accumulated dose of 55 electrons per Å2 at a pixel size of 1.15Å on the specimen. Defocus values ranged from −1.7 to −2.8μm. Further details are presented in Exended Data Table 3.
Falcon B., Zhang W., Murzin A.G., Murshudov G., Garringer H.J., Vidal R., Crowther R.A., Ghetti B., Scheres S.H, & Goedert M. (2018). Structures of filaments from Pick’s disease reveal a novel tau protein fold. Nature, 561(7721), 137-140.
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8

Cryo-EM analysis of Sei1 complexes

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Four microliters of purified Sei1 or Sei1-Ldb16 complex at a concentration of 4 mg/mL was adsorbed to glow-discharged gold UltrAufoil grids (300 mesh, R1.2/1.3) for 10 s. Grids were then blotted for 2 s at 100% humidity at 9 °C and frozen in liquid ethane using a Vitrobot Mark IV (Thermo Fisher Scientific). Data were collected in counting mode on a Titan Krios G3 (FEI) operating at 300 kV with a GIF energy filter (Gatan) and K2 Summit detector (Gatan) using a pixel size of 0.822 Å, a dose rate of 6 e− per Å2 per s and an exposure of 8 s, corresponding to a total dose of 48 e− per Å2 collected over 32 fractions.
Four microliters of purified Sei1∆231-243 (Sei1∆LH) at a concentration of 7.8 mg/ml was adsorbed to a glow-discharged gold UltrAufoil grid (300 mesh, R1.2/1.3) for 10 s. Grids were then blotted for 2 s at 100% humidity at 6 °C and frozen in liquid ethane using a Vitrobot Mark IV (Thermo Fisher Scientific). Data were collected in counted super-resolution mode on a Titan Krios G3 (FEI) operating at 300 kV with a BioQuantum imaging filter (Gatan) and K3 direct detection camera (Gatan) at 105,000× magnification, physical pixel size of 0.832 Å. Data were collected at a dose rate of 22.2 e− per Å2 per s and an exposure time of 2.66 s, corresponding to a total dose of 59.1 e− per Å2 collected over 40 fractions.
Klug Y.A., Deme J.C., Corey R.A., Renne M.F., Stansfeld P.J., Lea S.M, & Carvalho P. (2021). Mechanism of lipid droplet formation by the yeast Sei1/Ldb16 Seipin complex. Nature Communications, 12, 5892.
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9

Characterization of Tau Filaments

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Extracted tau filaments from frontal cortex were centrifuged at 3,000 g for 30 s, before being applied to glow-discharged holey carbon grids (Quantifoil Au R1.2/1.3, 300 mesh) and plunge-frozen in liquid ethane using a Thermo Fischer Vitrobot Mark IV. Images were acquired on a Gatan K2-Summit detector in counting mode using a Thermo Fischer Titan Krios microscope at 300 kV. A GIF-quantum energy filter (Gatan) was used with a slit width of 20 eV to remove inelastically scattered electrons. Further details are given in Extended Data Table 1. Filaments widths and crossover distances were measured manually in the cryo-EM micrographs. Statistical analyses on these measurements were performed using a one-way ANOVA test, followed by Tukey’s multiple comparisons test (Prism, GraphPad Software, Inc.).
Zhang W., Tarutani A., Newell K.L., Murzin A.G., Matsubara T., Falcon B., Vidal R., Garringer H.J., Shi Y., Ikeuchi T., Murayama S., Ghetti B., Hasegawa M., Goedert M, & Scheres S.H. (2020). Novel tau filament fold in corticobasal degeneration. Nature, 580(7802), 283-287.
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10

Characterization of Tau Filaments

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Extracted tau filaments from frontal cortex were centrifuged at 3,000 g for 30 s, before being applied to glow-discharged holey carbon grids (Quantifoil Au R1.2/1.3, 300 mesh) and plunge-frozen in liquid ethane using a Thermo Fischer Vitrobot Mark IV. Images were acquired on a Gatan K2-Summit detector in counting mode using a Thermo Fischer Titan Krios microscope at 300 kV. A GIF-quantum energy filter (Gatan) was used with a slit width of 20 eV to remove inelastically scattered electrons. Further details are given in Extended Data Table 1. Filaments widths and crossover distances were measured manually in the cryo-EM micrographs. Statistical analyses on these measurements were performed using a one-way ANOVA test, followed by Tukey’s multiple comparisons test (Prism, GraphPad Software, Inc.).
Zhang W., Tarutani A., Newell K.L., Murzin A.G., Matsubara T., Falcon B., Vidal R., Garringer H.J., Shi Y., Ikeuchi T., Murayama S., Ghetti B., Hasegawa M., Goedert M, & Scheres S.H. (2020). Novel tau filament fold in corticobasal degeneration. Nature, 580(7802), 283-287.
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