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Cs corrector

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The Cs corrector is a specialized component used in electron microscopy systems. Its core function is to correct for chromatic aberration, which occurs when electrons with different energies are focused differently by the microscope's electromagnetic lenses. By compensating for this aberration, the Cs corrector helps to improve the overall resolution and image quality of the electron microscope.

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Lab products found in correlation

Vitrobot mark 4, by Thermo Fisher Scientific (25 mentions) Titan krios microscope, by Thermo Fisher Scientific (5 mentions) Epu software, by Thermo Fisher Scientific (5 mentions) K2 summit direct electron detector, by Ametek (4 mentions) Quantum energy filter, by Thermo Fisher Scientific (3 mentions) Plasma cleaner, by Harrick (3 mentions) Quantum energy filter, by Ametek (3 mentions) Titan krios, by Ametek (3 mentions) K2 summit direct electron camera, by Ametek (2 mentions) Filter paper, by Ted Pella (2 mentions) R1 2 1, by Quantifoil (2 mentions) Bioquantum energy filter, by Ametek (2 mentions) Talos arctica, by Thermo Fisher Scientific (2 mentions) Krios microscope, by Thermo Fisher Scientific (1 mentions) Volta phase plate, by Thermo Fisher Scientific (1 mentions) Falcon 3 detector, by Thermo Fisher Scientific (1 mentions) Titan krios, by Thermo Fisher Scientific (1 mentions) Gatan k2 summit detector, by Thermo Fisher Scientific (1 mentions) Tecnai arctica microscope, by Thermo Fisher Scientific (1 mentions) Falcon 2 4k 4k camera, by Thermo Fisher Scientific (1 mentions)

18 protocols using cs corrector

1

Cryo-EM Structural Imaging Workflow

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Cryo-EM imaging was performed on a Titan Krios microscope operated at 300 kV (FEI) equipped with a Gatan K2 Summit direct electron camera (Gatan), a Gatan quantum energy filter, and a CS corrector (FEI). Images were recorded in EFTEM nanoprobe mode with Serial EM48 (link) in super-resolution counting mode with a super resolution pixel size of 0.55 Å and a defocus range of −1 to −3.2 µm. Six datasets were collected with a dose rate of 6–8 e−/pixel/s (1.1 Å pixel size at the specimen) on the detector. Images were recorded with a total dose of 50 electrons/Å2, exposure time between 7–10 and 0.2–0.25 s subframes (35–50 total frames).
Vanden Broeck A., Lotz C., Drillien R., Haas L., Bedez C, & Lamour V. (2021). Structural basis for allosteric regulation of Human Topoisomerase IIα. Nature Communications, 12, 2962.
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2

Cryo-EM Imaging of Biomolecular Complexes

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Cryo-EM imaging was performed on a Titan Krios microscope operated at 300 kV (FEI) equipped with a K2 Summit direct electron camera (Gatan), a GIF Quantum energy filter (Gatan) operated in zero-energy-loss mode with a slit width of 20 e−V, a Volta Phase Plate (FEI) and a CS corrector (FEI). Images were recorded in EFTEM nanoprobe mode with Serial EM53 (link) in super-resolution counting mode at nominal magnification of 130,000x with a super-resolution pixel size of 0.44 Å and a constant defocus target of −500 nm (Supplementary Fig. 2c). The VPP was advanced to a new position every 100 min (Supplementary Fig. 2b). Four datasets were collected with a dose rate of 6 to 8 e−/pixel/s (0.88 Å pixel size at the specimen) on the detector. Images were recorded with a total dose of 50 e−/Å2, exposure time between 7 to 10 s and 0.2 to 0.25 s subframes (35 to 50 total frames). A total of 11,833 movies were recorded after data collection of the 4 datasets.
Vanden Broeck A., Lotz C., Ortiz J, & Lamour V. (2019). Cryo-EM structure of the complete E. coli DNA gyrase nucleoprotein complex. Nature Communications, 10, 4935.
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3

High-Resolution Cryo-EM of Microtubule-Bound Proteins

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To improve the resolution of RS1 and RS2 bound to doublet microtubules from our previous report21 (link), we collected ~9,600 additional micrographs with the same imaging conditions. All data were collected using a 300 keV Titan Krios microscope equipped with a Cs-corrector (Thermo Fisher Scientific) and a BioQuantum Energy Filter (Gatan) at the Washington University in St. Louis Center for Cellular Imaging (WUCCI). All movies were recorded with a K2 Summit direct electron detector (Gatan) in counting mode, with an exposure rate of 8.5 electrons/pixel/s on the detector camera. The images were recorded at a nominal magnification of 81,000×, corresponding to a calibrated pixel size of 1.403 Å. A total exposure time of 9 s, corresponding to a total dose of 38.9 electrons/Å2 on the specimen, was fractionated into 30 movie frames. A defocus range from −1.0 to −3.5 μm was set during data acquisition. The data were collected automatically using EPU software (Thermo Fisher Scientific).
Gui M., Ma M., Sze-Tu E., Wang X., Koh F., Zhong E.D., Berger B., Davis J.H., Dutcher S.K., Zhang R, & Brown A. (2020). Structures of radial spokes and associated complexes important for ciliary motility. Nature structural & molecular biology, 28(1), 29-37.
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4

Cryo-EM Sample Preparation for TsFpn-Fab Nanodiscs

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The cryo grids were prepared using Thermo Fisher Vitrobot Mark IV. The Quantifoil R1.2/1.3 Cu grids were glow-discharged with air for 15 s at 10 mM in a Plasma Cleaner (PELCO EasiGlowTM). Aliquots of 3.5 µl purified TsFpn-Fab in nanodisc were applied to glow-discharged grids. After being blotted with filter paper (Ted Pella, Inc.) for 4.0 s, the grids were plunged into liquid ethane cooled with liquid nitrogen. A total of 1838 micrograph stacks were collected for TsFpn-Fab and 1381 for TsFpn-Fab-hepcidin with SerialEM41 (link) on a Titan Krios at 300 kV equipped with a K2 Summit direct electron detector (Gatan), a Quantum energy filter (Gatan) and a Cs corrector (Thermo Fisher), at a nominal magnification of 105,000× and defocus values from −2.0 µm to −1.2 µm. Each stack was exposed in the super-resolution mode for 5.6 s with an exposing time of 0.175 s per frame, resulting in 32 frames per stack. The total dose rate was about 50 e−/Å2 for each stack. The stacks were motion corrected with MotionCor242 (link) and binned 2 fold, resulting in a pixel size of 1.114 Å/pixel. In the meantime, dose weighting was performed43 (link). The defocus values were estimated with Gctf44 (link).
Pan Y., Ren Z., Gao S., Shen J., Wang L., Xu Z., Yu Y., Bachina P., Zhang H., Fan X., Laganowsky A., Yan N, & Zhou M. (2020). Structural basis of ion transport and inhibition in ferroportin. Nature Communications, 11, 5686.
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5

Cryo-EM Structure Determination of MrgD-Gi Complex

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The cryo-EM grids were prepared by applying 3.5 μL of the purified β-alanine-bound or apo MrgD–Gi complexes at ~15 mg mL−1 to glow-discharged holey carbon grids (Quantifoil R1.2/1.3, Au, 300 mesh). The grids were plunge-frozen in liquid ethane using a Vitrobot Mark IV (Thermo Fisher Scientific). The frozen grids were transferred to liquid nitrogen and stored for data acquisition. Cryo-EM imaging was performed at the Institute for Protein Research, Osaka University, on a Titan Krios instrument (Thermo Fisher Scientific) operating at an acceleration voltage of 300 kV and equipped with a Cs corrector (CEOS, GmbH). Movies were recorded using a K3 detector (Gatan) in CDS mode at a magnification of 105,000× at the camera level, corresponding to a pixel size of 0.675 Å with 66 frames at a dose of 0.91  e−/Å2 per frame and an exposure time of 3 s per movie resulting in a total dose of 60 e−/Å−2 s−1 with a defocus ranging from −0.7 to −1.9 μm. Data were automatically collected using the SerialEM software (https://bio3d.colorado.edu/SerialEM/) with an energy filter at a slit width of 20 eV. A total of 15,184 and 14,623 movies were collected for the β-alanine MrgD–Gi complex and the apo MrgD–Gi complex, respectively.
Suzuki S., Iida M., Hiroaki Y., Tanaka K., Kawamoto A., Kato T, & Oshima A. (2022). Structural insight into the activation mechanism of MrgD with heterotrimeric Gi-protein revealed by cryo-EM. Communications Biology, 5, 707.
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6

High-Resolution Cryo-EM of Microtubule-Bound Proteins

Cited 1 time
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To improve the resolution of RS1 and RS2 bound to doublet microtubules from our previous report21 (link), we collected ~9,600 additional micrographs with the same imaging conditions. All data were collected using a 300 keV Titan Krios microscope equipped with a Cs-corrector (Thermo Fisher Scientific) and a BioQuantum Energy Filter (Gatan) at the Washington University in St. Louis Center for Cellular Imaging (WUCCI). All movies were recorded with a K2 Summit direct electron detector (Gatan) in counting mode, with an exposure rate of 8.5 electrons/pixel/s on the detector camera. The images were recorded at a nominal magnification of 81,000×, corresponding to a calibrated pixel size of 1.403 Å. A total exposure time of 9 s, corresponding to a total dose of 38.9 electrons/Å2 on the specimen, was fractionated into 30 movie frames. A defocus range from −1.0 to −3.5 μm was set during data acquisition. The data were collected automatically using EPU software (Thermo Fisher Scientific).
Gui M., Ma M., Sze-Tu E., Wang X., Koh F., Zhong E.D., Berger B., Davis J.H., Dutcher S.K., Zhang R, & Brown A. (2020). Structures of radial spokes and associated complexes important for ciliary motility. Nature structural & molecular biology, 28(1), 29-37.
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7

Cryo-EM Sample Preparation for hDGAT1

Cited 3 times
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Cryo grids were prepared using the Thermo Fisher Vitrobot Mark IV. Quantifoil R1.2/1.3 Cu grids were glow-discharged in air for 40 sec at medium level using the Plasma Cleaner (Harrick Plasma, PDC-32G-2). 3.5 μl of concentrated hDGAT1 were applied to each glow-discharged grid. After blotting with filter paper (Ted Pella, Inc. Prod.# 47000–100) for 3.5 sec, the grids were plunged into liquid ethane cooled with liquid nitrogen. Movie stacks were collected using SerialEM23 (link) on a Titan Krios at 300 kV with a Quantum energy filter (Gatan) and a Cs corrector (Thermo Fisher), and at a nominal magnification of 105,000 × and defocus values of −2.0 μm to −1.2 μm. A K2 Summit direct electron detector (Gatan) was paired with the microscope. Each stack was collected in the super-resolution mode with an exposing time of 0.175 sec per frame for a total of 32 frames. The dose was about 50 e−/Å2 for each stack. The stacks were motion corrected with MotionCor224 (link) and binned (2×2) so that the pixel size is 1.114 Å. Dose weighting25 (link) was performed during motion correction, and the defocus values were estimated with Gctf26 (link).
Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V., Laganowsky A., Yan N, & Zhou M. (2020). Structure and mechanism of human diacylglycerol O-acyltransferase-1. Nature, 581(7808), 329-332.
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8

Cryo-EM of Doublet Microtubules

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The samples were applied to Quantifoil or C-flat R1.2/1.3 copper grids mounted in a Vitrobot Mark IV (Thermo Fisher Scientific) operated at 4°C and 95% humidity. Following blotting for 4 seconds, the grids were plunge frozen in liquid ethane.
Data were collected over 5 cryo-EM sessions using a 300 keV Titan Krios microscope equipped with a Cs-corrector (Thermo Fisher Scientific) and a Bioquantum Energy Filter (Gatan) at the Center for Cellular Imaging (WUCCI) in Washington University in St. Louis (WUSTL). All data (8,314 micrographs in total) were collected using a K2 Summit direct electron detector (Gatan) in counting mode, with an exposure rate of 8.5 electrons/pixel/s on the detector camera. The images were recorded at a nominal magnification of 81,000×, corresponding to a calibrated pixel size of 1.403 Å. A total exposure time of 9 s, corresponding to a total dose of 38.9 electrons/Å2 on the specimen, was fractionated into 30 movie frames. A defocus range from −1.0 to −3.5 μm was set during data acquistion. The data were collected automatically using EPU software (Thermo Fisher Scientific). The data collection statistics for doublet microtubules isolated from wild type cells are listed in Table S1. Statistics for the mutant strains can be found associated with their EMDB entries.
Ma M., Stoyanova M., Rademacher G., Dutcher S.K., Brown A, & Zhang R. (2019). Structure of the decorated ciliary doublet microtubule. Cell, 179(4), 909-922.e12.
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9

Cryo-EM of Horse PepT1 in Nanodiscs

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Quantifoil R1.2/1.3 Cu grids were applied with 3.5 μL of purified horse PepT1 in nanodisc at concentration of 5 or 10 mg/mL after glow-discharged with air for 15 seconds. The grids were plunged and frozen into liquid ethane cooled by liquid nitrogen after 6 second blotting at condition of 8 °C, 100% humidity using Vitrobot Mark IV (Thermo Fisher). A total of 2,531 multi-frame stacks were automatically collected with SerialEM (Mastronarde, 2005 (link)) on Titan Krios at 300 kV equipped with a K2 Summit direct electron detector (Gatan), a Quantum energy filter (Gatan) and Cs corrector (Thermo Fisher), at a nominal magnification of 105,000× with defocus range set to −2.1 μm to −1.9 μm. Each stack was exposed in super-resolution mode for 5.6 s with an exposure time of 0.175 s per frame, resulting in 32 frames per stack. The total dose was approximately 50 e−/Å2 for each stack.
Shen J., Hu M., Fan X., Ren Z., Portioli C., Yan X., Rong M, & Zhou M. (2022). Extracellular domain of PepT1 interacts with TM1 to facilitate substrate transport. Structure (London, England : 1993), 30(7), 1035-1041.e3.
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10

Cryo-EM Sample Preparation for hDGAT1

Cited 3 times
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Cryo grids were prepared using the Thermo Fisher Vitrobot Mark IV. Quantifoil R1.2/1.3 Cu grids were glow-discharged in air for 40 sec at medium level using the Plasma Cleaner (Harrick Plasma, PDC-32G-2). 3.5 μl of concentrated hDGAT1 were applied to each glow-discharged grid. After blotting with filter paper (Ted Pella, Inc. Prod.# 47000–100) for 3.5 sec, the grids were plunged into liquid ethane cooled with liquid nitrogen. Movie stacks were collected using SerialEM23 (link) on a Titan Krios at 300 kV with a Quantum energy filter (Gatan) and a Cs corrector (Thermo Fisher), and at a nominal magnification of 105,000 × and defocus values of −2.0 μm to −1.2 μm. A K2 Summit direct electron detector (Gatan) was paired with the microscope. Each stack was collected in the super-resolution mode with an exposing time of 0.175 sec per frame for a total of 32 frames. The dose was about 50 e−/Å2 for each stack. The stacks were motion corrected with MotionCor224 (link) and binned (2×2) so that the pixel size is 1.114 Å. Dose weighting25 (link) was performed during motion correction, and the defocus values were estimated with Gctf26 (link).
Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V., Laganowsky A., Yan N, & Zhou M. (2020). Structure and mechanism of human diacylglycerol O-acyltransferase-1. Nature, 581(7808), 329-332.
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