F20 electron microscope
The F20 electron microscope is a high-performance imaging tool designed for materials characterization. It utilizes an electron beam to produce high-resolution images of samples at the nanoscale level. The F20 provides detailed information about the structure and composition of materials, enabling researchers to gain a deeper understanding of their properties and behavior.
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10 protocols using f20 electron microscope
Cryo-EM Imaging of Protein Samples
In Vitro Reconstitution of Ctf3c-Cnn1-Ulp2 Complex
Protein concentration after gel filtration was measured by absorbance at 280 nm, and a fraction containing ∼0.5 µg/ml protein was selected for analysis by cryo-EM. 3.5 µl of the eluate was applied to a cryo-EM grid (C-flat 2/1, glow discharged for 30 s at 15 mA). The grid was plunged into liquid ethane after blotting from both sides for 4 s using a Cryoplunge 3 instrument (Gatan). Vitrified samples were screened for ice thickness and sample distribution using an F20 electron microscope (FEI) operating at 200 kV.
Negative Stain Microscopy of Outer Dynein Arms
Electron Microscopy Sample Preparation
Cryo-EM Structure Determination of FhuA-RBP pb5
Two different data sets were acquired on the same grid. For both data sets, 60-frame movies with a total dose of 60 e -/Å 2 were acquired on a ThermoFisher Scientific Titan Krios G3 transmission electron microscope (European Synchrotron Radiation Facility, Grenoble, France) (53) operated at 300 kV and equipped with a Gatan Quantum LS/967 energy filter (slit width of 20 eV used) coupled to a Gatan K2 summit direct electron detector. Automated data collection was performed using ThermoFisher Scientific EPU software. A nominal magnification of ×130,000 was used, resulting in a calibrated pixel size at the specimen level of 1.052 Å/pixel. For the first data set, 777 movies were acquired with a phase plate, close to focus (between -0.5 and -1.0 μm), while for the second data set, 8,752 movies were acquired without a phase plate and with a defocus ranging between -1.2 and -2.6 μm.
Nanoring Structural Determination by Cryo-EM
Contrast transfer function for each image was estimated using CTFFIND4 [68 (link)]. One thousand particles of nanorings were picked using XMIPP manual-picking utility within SCIPION framework [69 (link)]. Manually picked particles were used as input into XMIPP auto-picking utility, resulting in 13,861 particles. Particles were extracted and binned to have the box size of 100 pixels, corresponding to the pixel size of 4 Å; phase-flipped; and subjected for three rounds of reference-free 2D classification without contrast transfer function correction in RELION-3.0 Beta [70 (link)].
Non-cross-linked IkCON3 complex visualization
Structural Analysis of KAP1 Protein
Electron Microscopy Protocol for Structural Analysis
Visualizing VLP in Biofilms Using TEM
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