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In the 60-s of the XX century, the background for the current rapid development of cryo-electron microscopy has been established. At that time, single particle EM was used to determine 3D structures of large molecules in negative contrast. Later, cryo-EM helped to obtain three-dimensional structures of molecules with higher resolution. In the XXI century, accelerating voltages of electron microscopes have increased, field emission cathodes and modern electron-optical systems have appeared, improving the characteristics of the electron beam. Direct electron detectors opened up a new way of collecting the images. By 2019, more than 8000 protein 3D structures have been submitted to EMDB, including de-novo determined structures. Due to the constant modification of computer software, fully automated data collection and processing cryo-EM are now accessible to the wider scientific community.