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R1.2 1 3 300 mesh gold holey carbon grid

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The Quantifoil R1.2/1.3 300-mesh gold holey carbon grid is a sample support designed for transmission electron microscopy (TEM) applications. It features a regular pattern of holes within a carbon film, supported on a gold mesh grid. The core function of this product is to provide a stable and consistent support for specimens during TEM imaging and analysis.

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Lab products found in correlation

Vitrobot mark 4, by Thermo Fisher Scientific (11 mentions) Titan krios microscope, by Thermo Fisher Scientific (11 mentions) Epu software, by Thermo Fisher Scientific (4 mentions) K2 summit direct electron detector, by Ametek (1 mentions) K3 summit direct electron detector, by Ametek (1 mentions) K2 summit, by Thermo Fisher Scientific (1 mentions)

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Quantifoil holey carbon grids (59 citations) Quantifoil 2/2 grids (4 citations)

11 protocols using r1.2 1 3 300 mesh gold holey carbon grid

1

Cryo-EM imaging of MCU/EMRE-nanodisc complex

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The cryo-EM grids were prepared by applying 3 μL of the MCU/EMRE-nanodisc complex to a glow-discharged Quantifoil R1.2/1.3 300-mesh gold holey carbon grid (Quantifoil, Micro Tools GmbH, Germany) and blotted for 4.0 seconds under 100% humidity at 4 °C before being plunged into liquid ethane using a Mark IV Vitrobot (FEI). Micrographs were acquired on a Titan Krios microscope (FEI) operated at 300 kV with a K2 Summit direct electron detector (Gatan), using a slit width of 20 eV on a GIF-Quantum energy filter and a Volta phase plate (Danev, 2016 (link), 2017 (link)). EPU software (FEI) was used for automated data collection following standard FEI procedure. A calibrated magnification of 59,523x was used for imaging, yielding a pixel size of 0.84 Å on images. The defocus was set at −0.5 μm. Each micrograph was dose-fractionated to 30 frames under a dose rate of 4 e−/pixel/s, with a total exposure time of 12 s, resulting in a total dose of about 60 e−/Å2.
For the MCU-nanodisc sample, micrographs were acquired using a slit width of 20 eV on a GIF-Quantum energy. A calibrated magnification of 46,729x was used for imaging, yielding a pixel size of 1.07 Å on images. Each micrograph was dose-fractionated to 30 frames under a dose rate of 5 e−/pixel/s, with a total exposure time of 15 s.
Wang Y., Nguyen N.X., She J., Zeng W., Yang Y., Bai X.C, & Jiang Y. (2019). Structural mechanism of EMRE-dependent gating of the human mitochondrial calcium uniporter. Cell, 177(5), 1252-1261.e13.
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2

Cryo-EM Analysis of NCX1-Fab Complex

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Human NCX1-Fab 2E4 samples (5–6 mg/ml) in various conditions were applied to a glow-discharged Quantifoil R1.2/1.3 300-mesh gold holey carbon grid (Quantifoil, Micro Tools GmbH, Germany), blotted for 4.0 s under 100% humidity at 4 °C and plunged into liquid ethane using a Mark IV Vitrobot (FEI).
For the data of NCX1-Fab (2E4) samples in various states, movies were acquired on a Titan Krios microscope (FEI) operated at 300 kV with a K3 Summit direct electron detector (Gatan), using a slit width of 20 eV on a GIF-Quantum energy filter. Images were recorded with Serial EM in super-resolution counting mode with a super-resolution pixel size of 0.415 Å. The defocus range was set from −0.9 to −2.2 μm. Each movie was recorded for about 5 s in 60 subframes with a total dose of 60 e−/Å2. All data were collected using the CDS mode of the K3 camera with electron dose rates between 7 and 9 e-/pixel/s.
Xue J., Zeng W., Han Y., John S., Ottolia M, & Jiang Y. (2023). Structural mechanisms of the human cardiac sodium-calcium exchanger NCX1. Nature Communications, 14, 6181.
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3

Cryo-EM Structural Analysis of STING Protein

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Purified human and chicken STING of either the apo or cGAMP-bound form at 4.5 mg/ml was applied to a glow-discharged Quantifoil R1.2/1.3 300-mesh gold holey carbon grid (Quantifoil, Micro Tools), blotted under 100% humidity at 4 °C and plunged into liquid ethane using a Mark IV Vitrobot (FEI). Micrographs were acquired on a Titan Krios microscope (FEI) with a K2 Summit direct electron detector (Gatan) in the super-resolution counting mode, operated at 300 kV using the EPU software (FEI). The slit width of the GIF-Quantum energy filter was set to 20 eV. A Volta phase plate was used to enhance low-resolution features20 (link). Micrographs were dose-fractioned into 20 frames with a total exposure time of 10 s at the dose rate of 2 e− per pixel per second.
Shang G., Zhang C., Chen Z.J., Bai X.C, & Zhang X. (2019). Cryo-EM structures of STING reveal its mechanism of activation by cyclic GMP–AMP. Nature, 567(7748), 389-393.
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4

Cryo-EM Structure of A39R/PlexinC1 Complex

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The A39R/PlexinC1 complex in peptidiscs at 0.5 mg/ml was applied to a glow-discharged Quantifoil R1.2/1.3 300-mesh gold holey carbon grid (Quantifoil, Micro Tools GmbH, Germany), blotted under 100% humidity at 4 °C and plunged into liquid ethane using a Mark IV Vitrobot (FEI). Micrographs were collected on a Titan Krios microscope (FEI) with a K3 Summit direct electron detector (Gatan) operated at 300 kV using the SerialEM software32 (link). The GIF-Quantum energy filter was set to a slit width of 20 eV. Images were recorded in the super-resolution counting mode with the pixel size of 0.828 Å. Micrographs were dose-fractioned into 32 frames with the dose rate of 1.5 e−/Å/frame.
Kuo Y.C., Chen H., Shang G., Uchikawa E., Tian H., Bai X.C, & Zhang X. (2020). Cryo-EM structure of the PlexinC1/A39R complex reveals inter-domain interactions critical for ligand-induced activation. Nature Communications, 11, 1953.
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5

Cryo-EM Structure of Sema3A/PlexinA4/Nrp1 Complex

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The Sema3A/PlexinA4/Nrp1 complex at 2 mg/ml was applied to a glow-discharged Quantifoil R1.2/1.3 300-mesh gold holey carbon grid (Quantifoil, Micro Tools GmbH, Germany). The grid was blotted under 100% humidity at 4 °C and plunged into liquid ethane with a Mark IV Vitrobot (FEI). The serial EM software was used to control a 300 kV Titan Krios microscope (FEI) with a K3 Summit direct electron detector (Gatan) for Cryo-EM data collection52 (link). The slit width of the GIF-Quantum energy filter was set to 20 eV. Images were recorded in the super-resolution counting mode, dose-fractioned into 30 frames with the dose rate of 1.6 e−/Å/frame. The magnification was set to equivalent of the pixel size of 1.08 Å.
Lu D., Shang G., He X., Bai X.C, & Zhang X. (2021). Architecture of the Sema3A/PlexinA4/Neuropilin tripartite complex. Nature Communications, 12, 3172.
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6

Cryo-EM of NfMCU-saposin-Ru360 Complex

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Prior to freezing grids, the NfMCU saposin complex (concentrated to 0.6mg/mL) was incubated with 50μM Ru360 on ice for 30 minutes. The cryo-EM grids were prepared by applying 3 μL of the NfMCU-saposin-Ru360 complex to a glow-discharged Quantifoil R1.2/1.3 300-mesh gold holey carbon grid (Quantifoil, Micro Tools GmbH, Germany) and blotted for 4.0 seconds under 100% humidity at 4 °C before being plunged into liquid ethane using a Mark IV Vitrobot (FEI). Micrographs were acquired on a Titan Krios microscope (FEI) operated at 300 kV with a K2 Summit direct electron detector (Gatan), using a slit width of 20 eV on a GIF-Quantum energy filter as well as a Volta phase plate following the same approach for phase plate data collection as previously described33 (link). EPU software (FEI) was used for automated data collection following standard FEI procedure. A calibrated magnification of 59,523X was used for imaging, yielding a pixel size of 0.84 Å on images. The defocus was set at −0.5 μm. Each micrograph was dose-fractionated to 30 frames under a dose rate of 4 e−/pixel/s, with a total exposure time of 12 s, resulting in a total dose of about 60 e−/Å2.
Nguyen N.X., Armache J.P., Lee C., Yang Y., Zeng W., Mootha V.K., Cheng Y., Bai X.C, & Jiang Y. (2018). Cryo-EM structure of the mitochondrial calcium uniporter. Nature, 559(7715), 570-574.
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7

Cryo-EM Imaging of HsTMEM120A

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Purified HsTMEM120A at 5 mg/ml was applied to a glow-discharged Quantifoil R1.2/1.3 300-mesh gold holey carbon grid (Quantifoil, Micro Tools GmbH, Germany), blotted under 100% humidity at 4°C, and plunged into liquid ethane using a Mark IV Vitrobot (FEI).
Cryo-EM data were acquired on a Titan Krios microscope (FEI) at the HHMI Janelia Cryo-EM Facility operated at 300 kV with a K3 Summit direct electron detector (Gatan), using a slit width of 20 eV on a GIF Quantum energy filter. Images were recorded with Serial EM in super resolution counting mode with a super resolution pixel size of 0.422 Å. The defocus range was set from −0.9 to −2.2 μm. Each movie was dose-fractionated to 60 frames under a dose rate of 9.2 e-/pixel/s using CDS (Correlated Double Sampling) mode of the K3 camera, with a total exposure time of 4.646 s, resulting in a total dose of 60 e-/Å2.
Xue J., Han Y., Baniasadi H., Zeng W., Pei J., Grishin N.V., Wang J., Tu B.P, & Jiang Y. (2021). TMEM120A is a coenzyme A-binding membrane protein with structural similarities to ELOVL fatty acid elongase. eLife, 10, e71220.
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8

Cryo-EM of NfMCU-saposin-Ru360 Complex

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Prior to freezing grids, the NfMCU saposin complex (concentrated to 0.6mg/mL) was incubated with 50μM Ru360 on ice for 30 minutes. The cryo-EM grids were prepared by applying 3 μL of the NfMCU-saposin-Ru360 complex to a glow-discharged Quantifoil R1.2/1.3 300-mesh gold holey carbon grid (Quantifoil, Micro Tools GmbH, Germany) and blotted for 4.0 seconds under 100% humidity at 4 °C before being plunged into liquid ethane using a Mark IV Vitrobot (FEI). Micrographs were acquired on a Titan Krios microscope (FEI) operated at 300 kV with a K2 Summit direct electron detector (Gatan), using a slit width of 20 eV on a GIF-Quantum energy filter as well as a Volta phase plate following the same approach for phase plate data collection as previously described33 (link). EPU software (FEI) was used for automated data collection following standard FEI procedure. A calibrated magnification of 59,523X was used for imaging, yielding a pixel size of 0.84 Å on images. The defocus was set at −0.5 μm. Each micrograph was dose-fractionated to 30 frames under a dose rate of 4 e−/pixel/s, with a total exposure time of 12 s, resulting in a total dose of about 60 e−/Å2.
Nguyen N.X., Armache J.P., Lee C., Yang Y., Zeng W., Mootha V.K., Cheng Y., Bai X.C, & Jiang Y. (2018). Cryo-EM structure of the mitochondrial calcium uniporter. Nature, 559(7715), 570-574.
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9

Structural analysis of spike-Fab complex

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Purified spike ectodomain and SW186 Fab protein were mixed with the molar ratio of 1:4, and the mixture was incubated for 2 hours at 4 °C. After incubation, the sample was applied to Superose 6 10/300 Increase in SD buffer to remove excess Fab. Peak Fractions were collected and concentrated to 0.7 mg/mL, then applied to glow-discharged Quantifoil R1.2/1.3 300-mesh gold holey-carbon grids (Quantifoil, Micro Tools GmbH, Germany). Grids were blotted for 4 s under 100% humidity at 4 °C before being plunged into the liquid ethane using a Mark IV Vitrobot (FEI). Micrographs were acquired on a Titan Krios microscope (FEI) operated at 300 kV with a K3 direct electron detector (Gatan), using a slit width of 20 eV on a GIF-Quantum energy filter. SerialEM was used for the data collection. A calibrated magnification of 46,296 was used for imaging of the samples, yielding a pixel size of 1.08 Å on images. The defocus range was set from −1.6 μm to −2.6 μm. Each micrograph was dose-fractionated to 30 frames with a total dose of about 60 e-/Å2.
Fang Y., Sun P., Xie X., Du M., Du F., Ye J., Kalveram B.K., Plante J.A., Plante K.S., Li B., Bai X.C., Shi P.Y, & Chen Z.J. (2022). An antibody that neutralizes SARS-CoV-1 and SARS-CoV-2 by binding to a conserved spike epitope outside the receptor binding motif. Science Immunology.
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10

Cryo-EM Structure of Spike-Fab Complex

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Purified spike ectodomain and SW186 Fab protein were mixed with the molar ratio of 1:4, and the mixture was incubated for 2 hours at 4°C. After incubation, the sample was applied to Superose 6 10/300 Increase in SD buffer to remove excess Fab. Peak Fractions were collected and concentrated to 0.7 mg/mL, then applied to glow-discharged Quantifoil R1.2/1.3 300-mesh gold holey-carbon grids (Quantifoil, Micro Tools GmbH, Germany). Grids were blotted for 4 s under 100% humidity at 4°C before being plunged into the liquid ethane using a Mark IV Vitrobot (FEI). Micrographs were acquired on a Titan Krios microscope (FEI) operated at 300 kV with a K3 direct electron detector (Gatan), using a slit width of 20 eV on a GIF-Quantum energy filter. SerialEM was used for the data collection. A calibrated magnification of 46,296 was used for imaging of the samples, yielding a pixel size of 1.08 Å on images. The defocus range was set from -1.6 μm to -2.6 μm. Each micrograph was dose-fractionated to 30 frames with a total dose of about 60 e-/Å2.
Fang Y., Sun P., Xie X., Du M., Du F., Ye J., Kalveram B.K., Plante J.A., Plante K.S., Li B., Bai X.C., Shi P.Y, & Chen Z.J. (2022). An antibody that neutralizes SARS-CoV-1 and SARS-CoV-2 by binding to a conserved spike epitope outside the receptor binding motif. Science Immunology.
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