Genomics and Applied Biology 2024, Vol.15, No.1, 27-38 http://bioscipublisher.com/index.php/gab 29 Wang et al. (2020) argue that traditional electronic detectors are prone to damage when subjected to high-energy electron beam bombardment, which reduces the signal-to-noise ratio of imaging. However, with the invention and continuous optimization of electronic detectors, it is now possible to directly detect the number of electrons. The new electronic detectors have improved the imaging signal-to-noise ratio, continuously increasing the resolution of cryo electron microscopy and supporting the analysis of fine structures of biological macromolecules such as proteins. With the rapid development of computer technology, researchers are able to efficiently process and analyze cryoelectron microscopy images using more advanced algorithms, according to Vilas et al. (2022). These algorithms can automatically identify and correct errors in images, improving the accuracy and reliability of imaging. At the same time, the improvement of computing power also enables researchers to process larger datasets, accelerating the application process of cryo electron microscopy technology in protein structure analysis and other fields. 1.3 Recent technological progress Recently, cryoelectron microscopy technology has made significant technological progress in hardware, software, sample preparation technology, and application fields. These advances not only improve the performance and efficiency of cryoelectron microscopy technology, but also provide more accurate and efficient tools for research in fields such as protein structure analysis. With the continuous progress and improvement of technology, cryo electron microscopy technology will play a more important role in the future. Zhao et al. (2019) analyzed the structures of AMPA receptors in 10 different complexes in the brain using cryo EM, revealing the diversity of subunit composition and spatial configuration, providing new insights into the role of these receptors in rapid excitatory synaptic transmission. Watson et al. (2020) used cryoelectron microscopy technology to determine the structure of E. coli 70S ribosomes (Figure 1), with a global resolution of 2.0 Å. This work reveals the unambiguous localization of protein and RNA residues, their detailed chemical interactions, and chemical modifications, providing in-depth insights for future structural analysis. Figure 1 Section of Local Resolution Image of 70S Ribosome Reconstruction (Watson et al., 2020) Kordyukova et al. (2023) used a freeze transfer rack equipped with JEOL JEM-2100 transmission electron microscopy to investigate influenza A and B virus strains and their efficacy β- Preliminary cryoelectron microscopy data analysis was conducted on SARS-CoV-2 inactivated with propionate. These analyses help to distinguish virus particles with and without nucleocapsids, observe the lipid bilayer of the virus envelope, recognize influenza virus surface antigens and M1 protein layers, as well as the different morphologies of SARS-CoV-2 spinous processes.
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