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Solutions such as correlated cryo-fluorescence light microscopy, [19] and super-resolution light microscopy (e.g. cryo-PALM [20]) can be integrated with cryoET. In these techniques, a sample containing a fluorescently-tagged protein of interest is plunge-frozen and first imaged in a light microscope equipped with a special stage to allow the ...
Cryogenic electron microscopy (cryo-EM) is a cryomicroscopy technique applied on samples cooled to cryogenic temperatures. For biological specimens, the structure is preserved by embedding in an environment of vitreous ice .
In 2019, cryo-EM structures represented 2.5% of structures deposited in the Protein Data Bank, [6] and this number continues to grow. [7] An application of cryo-EM is cryo-electron tomography (cryo-ET), where a 3D reconstruction of the sample is created from tilted 2D images.
Electron tomography (ET) is a tomography technique for obtaining detailed 3D structures [1] of sub-cellular, macro-molecular, or materials specimens. Electron tomography is an extension of traditional transmission electron microscopy and uses a transmission electron microscope to collect the data.
Scanning electron cryomicroscopy (CryoSEM) is a form of electron microscopy where a hydrated but cryogenically fixed sample is imaged on a scanning electron microscope's cold stage in a cryogenic chamber.
MRC is a file format that has become an industry standard in cryo-electron microscopy (cryoEM) and electron tomography (ET), where the result of the technique is a three-dimensional grid of voxels each with a value corresponding to electron density or electric potential.
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The FSC originated in cryo-electron microscopy and gradually proliferated to other fields. To measure the FSC, two independently determined 3D volumes are required. In cryo-electron microscopy, the two volumes are the result of two three-dimensional reconstructions, each based on half of the available data set. Typically, random halves are used ...