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Journal articles on the topic 'Cryo-electron microscopy'

Author: Grafiati

Published: 4 June 2021

Last updated: 25 January 2025

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1

Stewart, Phoebe L. "Cryo-electron microscopy and cryo-electron tomography of nanoparticles." Wiley Interdisciplinary Reviews: Nanomedicine and Nanobiotechnology 9, no. 2 (June 23, 2016): e1417. http://dx.doi.org/10.1002/wnan.1417.

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2

Nijsse, Jaap, and Adriaan C. van Aelst. "Cryo-planing for cryo-scanning electron microscopy." Scanning 21, no. 6 (December 6, 2006): 372–78. http://dx.doi.org/10.1002/sca.4950210603.

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3

Lyu, Cheng-An, Yao Shen, and Peijun Zhang. "Zooming in and out: Exploring RNA Viral Infections with Multiscale Microscopic Methods." Viruses 16, no. 9 (September 23, 2024): 1504. http://dx.doi.org/10.3390/v16091504.

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RNA viruses, being submicroscopic organisms, have intriguing biological makeups and substantially impact human health. Microscopic methods have been utilized for studying RNA viruses at a variety of scales. In order of observation scale from large to small, fluorescence microscopy, cryo-soft X-ray tomography (cryo-SXT), serial cryo-focused ion beam/scanning electron microscopy (cryo-FIB/SEM) volume imaging, cryo-electron tomography (cryo-ET), and cryo-electron microscopy (cryo-EM) single-particle analysis (SPA) have been employed, enabling researchers to explore the intricate world of RNA viruses, their ultrastructure, dynamics, and interactions with host cells. These methods evolve to be combined to achieve a wide resolution range from atomic to sub-nano resolutions, making correlative microscopy an emerging trend. The developments in microscopic methods provide multi-fold and spatial information, advancing our understanding of viral infections and providing critical tools for developing novel antiviral strategies and rapid responses to emerging viral threats.

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4

Henderson, Richard, and Samar Hasnain. "`Cryo-EM': electron cryomicroscopy, cryo electron microscopy or something else?" IUCrJ 10, no. 5 (September 1, 2023): 519–20. http://dx.doi.org/10.1107/s2052252523006759.

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Structural biology continues to benefit from an expanding toolkit, which is helping to gain unprecedented insight into the assembly and organization of multi-protein machineries, enzyme mechanisms and ligand/inhibitor binding. During the last ten years, cryoEM has become widely available and has provided a major boost to structure determination of membrane proteins and large multi-protein complexes. Many of the structures have now been made available at resolutions around 2 Å, where fundamental questions regarding enzyme mechanisms can be addressed. Over the years, the abbreviation cryoEM has been understood to stand for different things. We wish the wider community to engage and clarify the definition of cryoEM so that the expanding literature involving cryoEM is unified.

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5

Weis, Felix, and Wim J. H. Hagen. "Combining high throughput and high quality for cryo-electron microscopy data collection." Acta Crystallographica Section D Structural Biology 76, no. 8 (July 27, 2020): 724–28. http://dx.doi.org/10.1107/s2059798320008347.

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Cryo-electron microscopy (cryo-EM) can be used to elucidate the 3D structure of macromolecular complexes. Driven by technological breakthroughs in electron-microscope and electron-detector development, coupled with improved image-processing procedures, it is now possible to reach high resolution both in single-particle analysis and in cryo-electron tomography and subtomogram-averaging approaches. As a consequence, the way in which cryo-EM data are collected has changed and new challenges have arisen in terms of microscope alignment, aberration correction and imaging parameters. This review describes how high-end data collection is performed at the EMBL Heidelberg cryo-EM platform, presenting recent microscope implementations that allow an increase in throughput while maintaining aberration-free imaging and the optimization of acquisition parameters to collect high-resolution data.

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6

Ye, Ke, and Lek-Heng Lim. "Cohomology of Cryo-Electron Microscopy." SIAM Journal on Applied Algebra and Geometry 1, no. 1 (January 2017): 507–35. http://dx.doi.org/10.1137/16m1070220.

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7

Doerr, Allison. "Single-particle cryo-electron microscopy." Nature Methods 13, no. 1 (December 30, 2015): 23. http://dx.doi.org/10.1038/nmeth.3700.

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8

Baker, Monya. "Cryo-electron microscopy shapes up." Nature 561, no. 7724 (September 2018): 565–67. http://dx.doi.org/10.1038/d41586-018-06791-6.

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9

Cossio, Pilar, and Edward Egelman. "Editorial overview: Cryo-electron microscopy." Current Opinion in Structural Biology 89 (December 2024): 102937. http://dx.doi.org/10.1016/j.sbi.2024.102937.

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10

Valentijn, JA, LF van Driel, AV Agronskaia, K. Knoops, RI Koning, M. Barcena, HC Gerritsen, and AJ Koster. "Novel Methods for Cryo-Fluorescence Microscopy Permitting Correlative Cryo-Electron Microscopy." Microscopy and Microanalysis 14, S2 (August 2008): 1314–15. http://dx.doi.org/10.1017/s1431927608086716.

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11

Wilkinson, Max E., Ananthanarayanan Kumar, and Ana Casañal. "Methods for merging data sets in electron cryo-microscopy." Acta Crystallographica Section D Structural Biology 75, no. 9 (August 23, 2019): 782–91. http://dx.doi.org/10.1107/s2059798319010519.

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Recent developments have resulted in electron cryo-microscopy (cryo-EM) becoming a useful tool for the structure determination of biological macromolecules. For samples containing inherent flexibility, heterogeneity or preferred orientation, the collection of extensive cryo-EM data using several conditions and microscopes is often required. In such a scenario, merging cryo-EM data sets is advantageous because it allows improved three-dimensional reconstructions to be obtained. Since data sets are not always collected with the same pixel size, merging data can be challenging. Here, two methods to combine cryo-EM data are described. Both involve the calculation of a rescaling factor from independent data sets. The effects of errors in the scaling factor on the results of data merging are also estimated. The methods described here provide a guideline for cryo-EM users who wish to combine data sets from the same type of microscope and detector.

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12

Busing, Wim M., and Marc J. C. de Jong. "The CM-CRYO: A Microscope Dedicated to Cryo-Electron Microscopy in Life Science Applications." Proceedings, annual meeting, Electron Microscopy Society of America 48, no. 1 (August 12, 1990): 176–77. http://dx.doi.org/10.1017/s0424820100179634.

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Low-temperature (cryo) electron microscopy has been established as a promising approach for alleviating technical problems encountered in electron microscopy of life science materials. Cryofixation freezes in the native situation of biological material, with the rapid freezing process preventing redistribution of water-soluble elements in cellular and non-cellular compartments. Thus it becomes possible to correlate tissue morphology with chemical and physical properties.The use of cryo techniques puts stringent demands on the electron microscope technology: an ultra-high vacuum, including special measures to tackle the water vapour released by the specimen; stable, low-drift cryo-temperature specimen holders; special functions providing low-dose imaging conditions; electron dose indicators; and a TV system for observation under low-level illumination. The new CM-CRYO combines these features with the ease of use of the CM microscope concept and the quality of the TWIN objective lens system.

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13

Tarassoli, Dr Seyedeh Zahra. "Cryo-Electron Microscopy in Dental Research." Journal of Medical Research and Surgery 5, no. 2 (April 3, 2024): 40–44. http://dx.doi.org/10.52916/jmrs244134.

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The field of dental research has experienced a significant transformation with the introduction of Cryo-Electron Microscopy (Cryo-EM), a technique that aims for accuracy and originality. This innovative imaging technology has surpassed the limitations of conventional microscopy, allowing for unique understanding of the complex structures and dynamic processes within the dental microcosm. This abstract explores the significant influence of Cryo-EM in dental research, specifically highlighting its crucial role in understanding the intricacies of dental tissues, interactions between biomaterials, and the behavior of microorganisms at the nanoscale. Cryo-EM combines advanced technology and scientific investigation to not only produce detailed images but also record the dynamic movements of molecules in dental biomaterials. This allows for the development of customized dental therapies. This abstract discusses the use of Cryo-EM in studying the structure of enamel, examining the interactions between dental materials and tissues, and analyzing the complex microbial communities in the mouth. Through the clarification of these intricate particulars, Cryo-EM emerges as a revolutionary instrument, molding the field of dental research, diagnostics, and therapeutic treatments. This investigation encompasses the wonders of Cryo-EM, enhancing our comprehension of dental complexities and laying the groundwork for groundbreaking progress in oral healthcare.

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14

McDowall, A. W., J. M. Smith, and J. Dubochet. "Thin sectioning for cryo transmission electron microscopy (cryo TEM)." Proceedings, annual meeting, Electron Microscopy Society of America 44 (August 1986): 102–3. http://dx.doi.org/10.1017/s0424820100142153.

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Processing whole cells and tissues for conventional TEM is known to cause structural alterations. Much effort has been devoted, therefore, to developing techniques which avoid specimen preparation artefacts. Recently, research using a cryo-electron microscope has shown that biological suspensions embedded in vitreous ice retain their structural integrity, and when compared with conventionally prepared TEM specimens, are free from many of the classical artefacts. In order to extend the advantage of cryo TEM to whole cells and tissues, we have developed a method of thin sectioning vitrified material.

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15

Vant, John W., Daipayan Sarkar, Jonathan Nguyen, Alexander T. Baker, Josh V. Vermaas, and Abhishek Singharoy. "Exploring cryo-electron microscopy with molecular dynamics." Biochemical Society Transactions 50, no. 1 (February 25, 2022): 569–81. http://dx.doi.org/10.1042/bst20210485.

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Single particle analysis cryo-electron microscopy (EM) and molecular dynamics (MD) have been complimentary methods since cryo-EM was first applied to the field of structural biology. The relationship started by biasing structural models to fit low-resolution cryo-EM maps of large macromolecular complexes not amenable to crystallization. The connection between cryo-EM and MD evolved as cryo-EM maps improved in resolution, allowing advanced sampling algorithms to simultaneously refine backbone and sidechains. Moving beyond a single static snapshot, modern inferencing approaches integrate cryo-EM and MD to generate structural ensembles from cryo-EM map data or directly from the particle images themselves. We summarize the recent history of MD innovations in the area of cryo-EM modeling. The merits for the myriad of MD based cryo-EM modeling methods are discussed, as well as, the discoveries that were made possible by the integration of molecular modeling with cryo-EM. Lastly, current challenges and potential opportunities are reviewed.

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16

Ma, Yue, J. Liang, Y. Zheng, S. L. Erlandsen, L. E. Scriven, and H. T. Davis. "Direct Imaging of Sodium Stearate Crystals Dispersed in Waterpropylene Glycol Mixtures by Cryo-Electron Microscopy." Microscopy and Microanalysis 7, S2 (August 2001): 734–35. http://dx.doi.org/10.1017/s1431927600029743.

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Cryo-scanning electron microscopy (cryo-SEM) and cryo-transmission electron microscopy (cryo- TEM), in conjunctions with rheological measurements, light and confocal microscopy, x-ray scattering, and solid state NMR, are used to characterize sodium stearate (NaSt) crystals dispersed in waterpropylene glycol (PG) mixtures at macroscopic, microscopic, molecular, and atomic levels. NaSt is a surface-active, structural agent in household and personal cleaning products, including deodorant sticks and soap bars. A better structural characterization of NaSt/PG/water systems has practical importance in personal care and cosmetic industries. NaSt crystals and other soap crystal morphologies have been studied by the TEM/replica technique. However, the replicas were made of the residue after the original sample or its aqueous dilution were dried, and the original structure may have been lost during drying. Cryo-SEM was not used to study NaSt crystals because of its lower resolution and because the crystals are highly susceptible to radiation damage by electron beam.

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17

Chung, Jeong Min, Clarissa L. Durie, and Jinseok Lee. "Artificial Intelligence in Cryo-Electron Microscopy." Life 12, no. 8 (August 19, 2022): 1267. http://dx.doi.org/10.3390/life12081267.

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Cryo-electron microscopy (cryo-EM) has become an unrivaled tool for determining the structure of macromolecular complexes. The biological function of macromolecular complexes is inextricably tied to the flexibility of these complexes. Single particle cryo-EM can reveal the conformational heterogeneity of a biochemically pure sample, leading to well-founded mechanistic hypotheses about the roles these complexes play in biology. However, the processing of increasingly large, complex datasets using traditional data processing strategies is exceedingly expensive in both user time and computational resources. Current innovations in data processing capitalize on artificial intelligence (AI) to improve the efficiency of data analysis and validation. Here, we review new tools that use AI to automate the data analysis steps of particle picking, 3D map reconstruction, and local resolution determination. We discuss how the application of AI moves the field forward, and what obstacles remain. We also introduce potential future applications of AI to use cryo-EM in understanding protein communities in cells.

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18

Czarnocki-Cieciura, Mariusz, and Marcin Nowotny. "Introduction to high-resolution cryo-electron microscopy." Postępy Biochemii 62, no. 3 (November 15, 2016): 383–94. http://dx.doi.org/10.18388/pb.2016_43.

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For many years two techniques have dominated structural biology â X-ray crystallography and NMR spectroscopy. Traditional cryo-electron microscopy of biological macromolecules produced macromolecular reconstructions at resolution limited to 6â10 Ă . Recent development of transmission electron microscopes, in particular the development of direct electron detectors, and continuous improvements in the available software, have led to the âresolution revolution” in cryo-EM. It is now possible to routinely obtain near-atomic-resolution 3D maps of intact biological macromolecules as small as ~100 kDa. Thus, cryo-EM is now becoming the method of choice for structural analysis of many complex assemblies that are unsuitable for structure determination by other methods.

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19

Erlandsen, Stanley L., Cecile Ottenwaelter, Chris Frethem, and Ya Chen. "Cryo Field Emission Scanning Electron Microscopy." BioTechniques 31, no. 2 (August 2001): 300–305. http://dx.doi.org/10.2144/01312bi01.

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20

Cai, Kai, Bryan S. Sibert, Anil Kumar, Jae Yang, Matt Larson, Keith Thompson, and Elizabeth R. Wright. "Cryo-Electron Microscopy of Extracellular Vesicles." Microscopy and Microanalysis 28, S1 (July 22, 2022): 1302–3. http://dx.doi.org/10.1017/s1431927622005347.

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21

Poweleit, Nicole. "Industry applications of cryo-electron microscopy." Acta Crystallographica Section A Foundations and Advances 78, a1 (July 29, 2022): a111. http://dx.doi.org/10.1107/s2053273322098886.

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22

Stark, Holger, and Reinhard Lührmann. "CRYO-ELECTRON MICROSCOPY OF SPLICEOSOMAL COMPONENTS." Annual Review of Biophysics and Biomolecular Structure 35, no. 1 (June 2006): 435–57. http://dx.doi.org/10.1146/annurev.biophys.35.040405.101953.

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23

Fitzpatrick, Anthony W. P., Ulrich J. Lorenz, Giovanni M. Vanacore, and Ahmed H. Zewail. "4D Cryo-Electron Microscopy of Proteins." Journal of the American Chemical Society 135, no. 51 (December 11, 2013): 19123–26. http://dx.doi.org/10.1021/ja4115055.

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24

Cressey, Daniel, and Ewen Callaway. "Cryo-electron microscopy wins chemistry Nobel." Nature 550, no. 7675 (October 2017): 167. http://dx.doi.org/10.1038/nature.2017.22738.

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25

Jiang, Bin, Conggang Li, and Maili Liu. "Progress in biomolecular cryo-electron microscopy." SCIENTIA SINICA Chimica 48, no. 3 (January 26, 2018): 277–81. http://dx.doi.org/10.1360/n032017-00195.

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26

Peplow, Mark. "Cryo-Electron Microscopy Reaches Resolution Milestone." ACS Central Science 6, no. 8 (August 18, 2020): 1274–77. http://dx.doi.org/10.1021/acscentsci.0c01048.

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27

Herzik Jr, Mark A. "Cryo-electron microscopy reaches atomic resolution." Nature 587, no. 7832 (October 21, 2020): 39–40. http://dx.doi.org/10.1038/d41586-020-02924-y.

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28

Costello, M. Joseph. "Cryo-Electron Microscopy of Biological Samples." Ultrastructural Pathology 30, no. 5 (January 2006): 361–71. http://dx.doi.org/10.1080/01913120600932735.

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29

Mooney, Paul. "Improving Detectors for Cryo-Electron Microscopy." Microscopy and Microanalysis 23, S1 (July 2017): 832–33. http://dx.doi.org/10.1017/s1431927617004822.

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30

Briegel, A. "Correlative Light and Electron Cryo-Microscopy." Microscopy and Microanalysis 18, S2 (July 2012): 1972–73. http://dx.doi.org/10.1017/s1431927612011713.

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31

Thonghin, Nopnithi, Vasileios Kargas, Jack Clews, and Robert C. Ford. "Cryo-electron microscopy of membrane proteins." Methods 147 (September 2018): 176–86. http://dx.doi.org/10.1016/j.ymeth.2018.04.018.

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32

Zhang, W., N. H. Olson, B. R. McKinney, R. J. Kuhn, and T. S. Baker. "Cryo-Electron Microscopy of Aura Viruses." Microscopy and Microanalysis 4, S2 (July 1998): 946–47. http://dx.doi.org/10.1017/s1431927600024855.

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Alphaviruses are a group of enveloped viruses in the Togaviridae family. Studies of several alphaviruses, including Ross River, Sindbis and Semliki Forest viruses, by cryo-electron microscopy (cryo-EM), three-dimensional (3D) image resconstruction and other techniques have illustrated that these spherical viruses have a T=4, multi-layered structure.Aura virus, which is closely related to Sindbis, was first isolated in South America. Unlike the other alphaviruses, both genomic RNA (12kb, 49S) and subgenomic RNA(4.2kb, 26S) are encapsidated efficiently and form mature virions. Studies on negatively-stained virus particles demonstrated that there are two major size classes. The first contains particles of ∼72nm diameter, which are most similar to wild type virus, whereas the second class includes particles of ∼62nm in diameter. The 72nm particles are believed to have one copy of genomic RNA or one to three copies of subgenomic RNA, and a T=4 structure. The 62nm particles probably only have a single copy of subgenomic RNA and are presumed to be T=3 structures.

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33

Dubochet, Jacques. "Life, Liquids and Cryo-Electron Microscopy." Europhysics News 18, no. 4 (1987): 54–56. http://dx.doi.org/10.1051/epn/19871804054.

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34

Wilson, Marcus D., and Alessandro Costa. "Cryo-electron microscopy of chromatin biology." Acta Crystallographica Section D Structural Biology 73, no. 6 (April 20, 2017): 541–48. http://dx.doi.org/10.1107/s2059798317004430.

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The basic unit of chromatin, the nucleosome core particle (NCP), controls how DNA in eukaryotic cells is compacted, replicated and read. Since its discovery, biochemists have sought to understand how this protein–DNA complex can help to control so many diverse tasks. Recent electron-microscopy (EM) studies on NCP-containing assemblies have helped to describe important chromatin transactions at a molecular level. With the implementation of recent technical advances in single-particle EM, our understanding of how nucleosomes are recognized and read looks to take a leap forward. In this review, the authors highlight recent advances in the architectural understanding of chromatin biology elucidated by EM.

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35

Al-Amoudi, Ashraf, Jiin-Ju Chang, Amélie Leforestier, Alasdair McDowall, Laurée Michel Salamin, Lars P. O. Norlén, Karsten Richter, Nathalie Sartori Blanc, Daniel Studer, and Jacques Dubochet. "Cryo-electron microscopy of vitreous sections." EMBO Journal 23, no. 18 (August 19, 2004): 3583–88. http://dx.doi.org/10.1038/sj.emboj.7600366.

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36

Glaeser, Robert M. "Cryo-electron microscopy of biological nanostructures." Physics Today 61, no. 1 (January 2008): 48–54. http://dx.doi.org/10.1063/1.2835153.

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37

Dubochet, Jacques, Marc Adrian, Jiin-Ju Chang, Jean-Claude Homo, Jean Lepault, Alasdair W. McDowall, and Patrick Schultz. "Cryo-electron microscopy of vitrified specimens." Quarterly Reviews of Biophysics 21, no. 2 (May 1988): 129–228. http://dx.doi.org/10.1017/s0033583500004297.

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Cryo-electron microscopy of vitrified specimens was just emerging as a practical method when Richard Henderson proposed that we should teach an EMBO course on the new technique. The request seemed to come too early because at that moment the method looked more like a laboratory game than a useful tool. However, during the months which ellapsed before the start of the course, several of the major difficulties associated with electron microscopy of vitrified specimens found surprisingly elegant solutions or simply became non-existent. The course could therefore take place under favourable circumstances in the summer of 1983. It was repeated the following years and cryo-electron microscopy spread rapidly. Since that time, water, which was once the arch enemy of all electronmicroscopists, became what it always was in nature – an integral part of biological matter and a beautiful substance.

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38

Hezel, U. B., E. Zellman, and D. Hoffmeister. "High-performance cryo transmission electron microscopy." Ultramicroscopy 17, no. 2 (January 1985): 174. http://dx.doi.org/10.1016/0304-3991(85)90043-9.

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39

Wang, Hong-Wei, Jianlin Lei, and Yigong Shi. "Biological cryo-electron microscopy in China." Protein Science 26, no. 1 (September 2, 2016): 16–31. http://dx.doi.org/10.1002/pro.3018.

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40

Lorenz, Ulrich J. "Microsecond time-resolved cryo-electron microscopy." Current Opinion in Structural Biology 87 (August 2024): 102840. http://dx.doi.org/10.1016/j.sbi.2024.102840.

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41

Chen, Xin. "Applications of Cryogenic Electron Microscopy in Characterizing Electrochemical Materials and Interfaces." Highlights in Science, Engineering and Technology 96 (May 5, 2024): 14–20. http://dx.doi.org/10.54097/7csg5b12.

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Cryogenic electron microscopy (cryo-EM) has emerged as a pivotal technology in materials science, particularly in characterizing electrochemical materials and interfaces. This paper delves into the recent advancements and applications of cryo-EM, underscoring its significance in understanding the intricate structures and mechanisms of materials sensitive to air and electron beams, such as lithium-ion battery electrodes. Cryo-EM's ability to capture materials in a near-natural state using vitreous ice and its compatibility with advanced imaging techniques like cryo-electron energy loss spectroscopy (cryo-EELS), cryo-electron tomography (cryo-ET), and cryo-focused ion beam (cryo-FIB) enhances our understanding of quantum and energy materials. This research will discuss the revolutionary impact of cryo-EM in areas like energy conservation and conversion, highlighting its role in visualizing sensitive materials and electrochemical reaction processes. This research addresses the need for comprehensive discussions on the characterization of quantum and energy materials through cryo-EM and related techniques, offering a thorough overview of recent advancements in this rapidly evolving field.

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Schwartz, CL. "Cryo-Fluorescence: A Tool for Correlative Cryo-Light and Cryo-Electron Microscopy." Microscopy and Microanalysis 14, S2 (August 2008): 744–45. http://dx.doi.org/10.1017/s143192760808522x.

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43

Chiu, Wah, Michael F. Schmid, Joanita Jakana, and Paul Matsudaira. "Electron cryo-microscopy of macromolecular assembly at 400 kV." Proceedings, annual meeting, Electron Microscopy Society of America 49 (August 1991): 426–27. http://dx.doi.org/10.1017/s042482010008643x.

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Electron cryo-microscopy has proven to be a valuable technique for determining 3-dimensional structures of biological macromolecules. The cryo technique is capable of preserving biological specimens in their native conformation and of reducing radiation damage during the microscopic observation. Computer processing is used to combine data from different angular views for 3-dimensional reconstruction. The structural detail revealed in this type of analysis can be limited by the quality of the electron microscopic images and the computational procedures used to retrieve the low contrast signals. So far, the highest resolution study of electron cryo-microscopy is bacteriorhodopsin where the polypeptide chain can be traced and some of the amino acid side chains can be identified. Though high resolution structure can be obtained by electron crystallographic analysis, further improvement can be made in several areas. These include specimen flatness, specimen movement induced by the electrons, and achievement of better signal to noise ratios in the images.

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44

Dillard, Rebecca S., Cheri M. Hampton, Joshua D. Strauss, Zunlong Ke, Deanna Altomara, Ricardo C. Guerrero-Ferreira, Gabriella Kiss, and Elizabeth R. Wright. "Biological Applications at the Cutting Edge of Cryo-Electron Microscopy." Microscopy and Microanalysis 24, no. 4 (August 2018): 406–19. http://dx.doi.org/10.1017/s1431927618012382.

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AbstractCryo-electron microscopy (cryo-EM) is a powerful tool for macromolecular to near-atomic resolution structure determination in the biological sciences. The specimen is maintained in a near-native environment within a thin film of vitreous ice and imaged in a transmission electron microscope. The images can then be processed by a number of computational methods to produce three-dimensional information. Recent advances in sample preparation, imaging, and data processing have led to tremendous growth in the field of cryo-EM by providing higher resolution structures and the ability to investigate macromolecules within the context of the cell. Here, we review developments in sample preparation methods and substrates, detectors, phase plates, and cryo-correlative light and electron microscopy that have contributed to this expansion. We also have included specific biological applications.

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45

Schwartz, CL, MS Ladinsky, and A. Hoenger. "Correlative Cryo-Light and Cryo-Electron Microscopy of Vitreous Sections." Microscopy and Microanalysis 14, S2 (August 2008): 1060–61. http://dx.doi.org/10.1017/s1431927608085243.

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46

Mitra, Alok K. "Visualization of biological macromolecules at near-atomic resolution: cryo-electron microscopy comes of age." Acta Crystallographica Section F Structural Biology Communications 75, no. 1 (January 1, 2019): 3–11. http://dx.doi.org/10.1107/s2053230x18015133.

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Structural biology is going through a revolution as a result of transformational advances in the field of cryo-electron microscopy (cryo-EM) driven by the development of direct electron detectors and ultrastable electron microscopes. High-resolution cryo-EM images of isolated biomolecules (single particles) suspended in a thin layer of vitrified buffer are subjected to powerful image-processing algorithms, enabling near-atomic resolution structures to be determined in unprecedented numbers. Prior to these advances, electron crystallography of two-dimensional crystals and helical assemblies of proteins had established the feasibility of atomic resolution structure determination using cryo-EM. Atomic resolution single-particle analysis, without the need for crystals, now promises to resolve problems in structural biology that were intractable just a few years ago.

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47

Vénien-Bryan, Catherine, Zhuolun Li, Laurent Vuillard, and Jean Albert Boutin. "Cryo-electron microscopy and X-ray crystallography: complementary approaches to structural biology and drug discovery." Acta Crystallographica Section F Structural Biology Communications 73, no. 4 (March 29, 2017): 174–83. http://dx.doi.org/10.1107/s2053230x17003740.

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The invention of the electron microscope has greatly enhanced the view scientists have of small structural details. Since its implementation, this technology has undergone considerable evolution and the resolution that can be obtained for biological objects has been extended. In addition, the latest generation of cryo-electron microscopes equipped with direct electron detectors and software for the automated collection of images, in combination with the use of advanced image-analysis methods, has dramatically improved the performance of this technique in terms of resolution. While calculating a sub-10 Å resolution structure was an accomplishment less than a decade ago, it is now common to generate structures at sub-5 Å resolution and even better. It is becoming possible to relatively quickly obtain high-resolution structures of biological molecules, in particular large ones (>500 kDa) which, in some cases, have resisted more conventional methods such as X-ray crystallography or nuclear magnetic resonance (NMR). Such newly resolved structures may, for the first time, shed light on the precise mechanisms that are essential for cellular physiological processes. The ability to attain atomic resolution may support the development of new drugs that target these proteins, allowing medicinal chemists to understand the intimacy of the relationship between their molecules and targets. In addition, recent developments in cryo-electron microscopy combined with image analysis can provide unique information on the conformational variability of macromolecular complexes. Conformational flexibility of macromolecular complexes can be investigated using cryo-electron microscopy and multiconformation reconstruction methods. However, the biochemical quality of the sample remains the major bottleneck to routine cryo-electron microscopy-based determination of structures at very high resolution.

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Han, Sung Sik. "Cryo-Transmission Electron Microscopy in Korean Society of Microscopy." Applied Microscopy 47, no. 4 (December 30, 2017): 215–17. http://dx.doi.org/10.9729/am.2017.47.4.215.

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Raimondi, Vittoria, and Alessandro Grinzato. "A basic introduction to single particles cryo-electron microscopy." AIMS Biophysics 9, no. 1 (2021): 5–20. http://dx.doi.org/10.3934/biophy.2022002.

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<abstract> <p>In the last years, cryogenic-electron microscopy (cryo-EM) underwent the most impressive improvement compared to other techniques used in structural biology, such as X-ray crystallography and NMR. Electron microscopy was invented nearly one century ago but, up to the beginning of the last decades, the 3D maps produced through this technique were poorly detailed, justifying the term “blobbology” to appeal to cryo-EM. Recently, thanks to a new generation of microscopes and detectors, more efficient algorithms, and easier access to computational power, single particles cryo-EM can routinely produce 3D structures at resolutions comparable to those obtained with X-ray crystallography. However, unlike X-ray crystallography, which needs crystallized proteins, cryo-EM exploits purified samples in solution, allowing the study of proteins and protein complexes that are hard or even impossible to crystallize. For these reasons, single-particle cryo-EM is often the first choice of structural biologists today. Nevertheless, before starting a cryo-EM experiment, many drawbacks and limitations must be considered. Moreover, in practice, the process between the purified sample and the final structure could be trickier than initially expected. Based on these observations, this review aims to offer an overview of the principal technical aspects and setups to be considered while planning and performing a cryo-EM experiment.</p> </abstract>

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Fujiyoshi, Yoshinori. "High-Resolution Cryo-Electron Microscopy of Biological Macromolecules." Proceedings, annual meeting, Electron Microscopy Society of America 48, no. 1 (August 12, 1990): 126–27. http://dx.doi.org/10.1017/s0424820100179385.

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The resolution of direct images of biological macromolecules is normally restricted to far less than 0.3 nm. This is not due instrumental resolution, but irradiation damage. The damage to biological macromolecules may expect to be reduced when they are cooled to a very low temperature. We started to develop a new cryo-stage for a high resolution electron microscopy in 1983, and successfully constructed a superfluid helium stage for a 400 kV microscope by 1986, whereby chlorinated copper-phthalocyanine could be photographed to a resolution of 0.26 nm at a stage temperature of 1.5 K. We are continuing to develop the cryo-microscope and have developed a cryo-microscope equipped with a superfluid helium stage and new cryo-transfer device.The New cryo-microscope achieves not only improved resolution but also increased operational ease. The construction of the new super-fluid helium stage is shown in Fig. 1, where the cross sectional structure is shown parallel to an electron beam path. The capacities of LN2 tank, LHe tank and the pot are 1400 ml, 1200 ml and 3 ml, respectively. Their surfaces are placed with gold to minimize thermal radiation. Consumption rates of liquid nitrogen and liquid helium are 170 ml/hour and 140 ml/hour, respectively. The working time of this stage is more than 7 hours starting from full LN2 and LHe tanks. Instrumental resolution of our cryo-stage cooled to 4.2 K was confirmed to be 0.20 nm by an optical diffraction pattern from the image of a chlorinated copper-phthalocyanine crystal. The image and the optical diffraction pattern are shown in Fig. 2 a, b, respectively.

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