Genomics and Applied Biology 2024, Vol.15, No.1, 27-38 http://bioscipublisher.com/index.php/gab 36 the accuracy issues currently reduced during sample transfer processes. The combination of computational simulation techniques, especially molecular dynamics simulations, further expands the application of cryo electron microscopy. This technology can reveal the dynamic characteristics and functional mechanisms of protein structure based on experimental data from cryo electron microscopy, providing a new perspective for understanding how biomolecules respond to environmental changes. Through this interdisciplinary combination, scientists are not only able to analyze protein structure and function in a more precise way, but also accelerate the transformation process from basic research to applied research. 5 Challenges and Prospects Cryo EM technology, as a powerful tool in biomedical research, has shown great potential in the field of protein and macromolecular complex structure analysis. However, in the pursuit of deeper understanding of biomolecules, Cryo EM still faces many challenges, especially in sample preparation, data collection and processing (Kühlbrandt, 2022). The difficulty of sample preparation, especially in rapidly freezing samples to preserve their structure close to the original ecology without forming ice crystals, and finding suitable preparation methods for proteins that are difficult to express or stable, is a major challenge. In addition, although the development of automated data collection systems has improved the efficiency of data collection, it has come with challenges in managing, storing, and analyzing large amounts of data, requiring continuous technological innovation and software development to optimize this process. Despite these challenges, Cryo EM still has extremely broad prospects in future biomedical research. Especially in analyzing the structures of large-sized and complex macromolecular complexes as well as low abundance proteins, Cryo EM can provide valuable information that helps to gain a deeper understanding of biological processes. With the advancement of technology, especially innovation in sample preparation techniques and image processing software, Cryo EM's ability to capture low abundance proteins and transient complex structures will be greatly enhanced, further promoting research in areas such as cell signal transduction and protein interactions. The combination of Cryo-EM with other structural biology techniques such as X-ray crystallography and nuclear magnetic resonance (NMR) (Tsegaye et al., 2021) will open up new research avenues. This cross technology integration not only breaks through the limitations of a single technology and provides more accurate and dynamic structural information, but also provides a more comprehensive perspective for the study of the structure and function of biological macromolecules, accelerating the transformation from basic research to applied research. With the continuous development and improvement of these technologies, the role of Cryo-EM in the field of life sciences will become more important in the future, providing strong impetus for revealing the mysteries of the biomolecular world. References Baker L., Grange M., and Grünewald K., 2017, Electron cryo-tomography captures macromolecular complexes in native environments.. Current opinion in structural biology, 46: 149-156. https://doi.org/10.1016/j.sbi.2017.08.005 Bonomi M., and Vendruscolo M., 2017, Simultaneous determination of protein structure and dynamics using cryo-electron microscopy, Biophysical Journal, 114: 1604-1613. https://doi.org/10.1016/j.bpj.2018.02.028 Chen S., Shi D., Sadiq M., and Cheng X., 2020, Image denoising with generative adversarial networks and its application to cell image enhancement. IEEE Access, 8: 82819-82831. https://doi.org/10.1109/ACCESS.2020.2988284 Cheng Y., Grigorieff N., Penczek P., and Walz T., 2015, A primer to single-particle cryo-electron microscopy, Cell, 161: 438-449. https://doi.org/10.1016/j.cell.2015.03.050 Chlanda P., and Locker J., 2017, The sleeping beauty kissed awake: new methods in electron microscopy to study cellular membranes, The Biochemical Journal, 474(6): 1041-1053. https://doi.org/10.1042/BCJ20160990 Costa T., Ignatiou A., and Orlova E., 2017, Structural analysis of protein complexes by cryo electron microscopy, Methods in Molecular Biology, 1615: 377-413. https://doi.org/10.1007/978-1-4939-7033-9_28
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