[{"main_file_link":[{"url":"https://doi.org/10.1093/jmicro/dfab048","open_access":"1"}],"status":"public","user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","type":"journal_article","date_published":"2022-03-01T00:00:00Z","publication_identifier":{"issn":["2050-5698"],"eissn":["2050-5701"]},"oa":1,"language":[{"iso":"eng"}],"publication":"Microscopy","project":[{"call_identifier":"H2020","_id":"25CA28EA-B435-11E9-9278-68D0E5697425","name":"In situ analysis of single channel subunit composition in neurons: physiological implication in synaptic plasticity and behaviour","grant_number":"694539"}],"oa_version":"Published Version","month":"03","volume":71,"acknowledgement":"European Research Council Advanced Grant (694539 to R.S.).","year":"2022","citation":{"apa":"Shigemoto, R. (2022). Electron microscopic visualization of single molecules by tag-mediated metal particle labeling. <i>Microscopy</i>. Oxford Academic. <a href=\"https://doi.org/10.1093/jmicro/dfab048\">https://doi.org/10.1093/jmicro/dfab048</a>","ama":"Shigemoto R. Electron microscopic visualization of single molecules by tag-mediated metal particle labeling. <i>Microscopy</i>. 2022;71(Supplement_1):i72-i80. doi:<a href=\"https://doi.org/10.1093/jmicro/dfab048\">10.1093/jmicro/dfab048</a>","chicago":"Shigemoto, Ryuichi. “Electron Microscopic Visualization of Single Molecules by Tag-Mediated Metal Particle Labeling.” <i>Microscopy</i>. Oxford Academic, 2022. <a href=\"https://doi.org/10.1093/jmicro/dfab048\">https://doi.org/10.1093/jmicro/dfab048</a>.","ieee":"R. Shigemoto, “Electron microscopic visualization of single molecules by tag-mediated metal particle labeling,” <i>Microscopy</i>, vol. 71, no. Supplement_1. Oxford Academic, pp. i72–i80, 2022.","mla":"Shigemoto, Ryuichi. “Electron Microscopic Visualization of Single Molecules by Tag-Mediated Metal Particle Labeling.” <i>Microscopy</i>, vol. 71, no. Supplement_1, Oxford Academic, 2022, pp. i72–80, doi:<a href=\"https://doi.org/10.1093/jmicro/dfab048\">10.1093/jmicro/dfab048</a>.","short":"R. Shigemoto, Microscopy 71 (2022) i72–i80.","ista":"Shigemoto R. 2022. Electron microscopic visualization of single molecules by tag-mediated metal particle labeling. Microscopy. 71(Supplement_1), i72–i80."},"date_updated":"2023-08-03T06:08:01Z","external_id":{"pmid":["35275179"],"isi":["000768384100011"]},"isi":1,"day":"01","doi":"10.1093/jmicro/dfab048","abstract":[{"lang":"eng","text":"Genetically encoded tags have introduced extensive lines of application from purification of tagged proteins to their visualization at the single molecular, cellular, histological and whole-body levels. Combined with other rapidly developing technologies such as clustered regularly interspaced palindromic repeats (CRISPR)/CRISPR-associated protein 9 (Cas9) system, proteomics, super-resolution microscopy and proximity labeling, a large variety of genetically encoded tags have been developed in the last two decades. In this review, I focus on the current status of tag development for electron microscopic (EM) visualization of proteins with metal particle labeling. Compared with conventional immunoelectron microscopy using gold particles, tag-mediated metal particle labeling has several advantages that could potentially improve the sensitivity, spatial and temporal resolution, and applicability to a wide range of proteins of interest (POIs). It may enable researchers to detect single molecules in situ, allowing the quantitative measurement of absolute numbers and exact localization patterns of POI in the ultrastructural context. Thus, genetically encoded tags for EM could revolutionize the field as green fluorescence protein did for light microscopy, although we still have many challenges to overcome before reaching this goal."}],"ec_funded":1,"quality_controlled":"1","page":"i72-i80","publisher":"Oxford Academic","article_type":"original","scopus_import":"1","pmid":1,"_id":"10889","issue":"Supplement_1","author":[{"id":"499F3ABC-F248-11E8-B48F-1D18A9856A87","first_name":"Ryuichi","last_name":"Shigemoto","orcid":"0000-0001-8761-9444","full_name":"Shigemoto, Ryuichi"}],"department":[{"_id":"RySh"}],"article_processing_charge":"No","date_created":"2022-03-20T23:01:39Z","publication_status":"published","intvolume":"        71","title":"Electron microscopic visualization of single molecules by tag-mediated metal particle labeling"},{"oa_version":"Published Version","month":"10","publication":"Microscopy","has_accepted_license":"1","language":[{"iso":"eng"}],"keyword":["Radiology","Nuclear Medicine and imaging","Instrumentation","Structural Biology"],"publication_identifier":{"issn":["2050-5698"],"eissn":["2050-5701"]},"oa":1,"tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)"},"date_published":"2022-10-01T00:00:00Z","type":"journal_article","file":[{"creator":"dernst","file_id":"12498","success":1,"access_level":"open_access","relation":"main_file","content_type":"application/pdf","file_name":"2022_Microscopy_Gerle.pdf","date_updated":"2023-02-03T08:34:48Z","checksum":"23b51c163636bf9313f7f0818312e67e","file_size":7812696,"date_created":"2023-02-03T08:34:48Z"}],"user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","status":"public","publication_status":"published","department":[{"_id":"LeSa"}],"date_created":"2022-07-25T10:04:58Z","article_processing_charge":"No","title":"Structures of multisubunit membrane complexes with the CRYO ARM 200","intvolume":"        71","pmid":1,"_id":"11648","scopus_import":"1","author":[{"last_name":"Gerle","first_name":"Christoph","full_name":"Gerle, Christoph"},{"full_name":"Kishikawa, Jun-ichi","first_name":"Jun-ichi","last_name":"Kishikawa"},{"full_name":"Yamaguchi, Tomoko","last_name":"Yamaguchi","first_name":"Tomoko"},{"last_name":"Nakanishi","first_name":"Atsuko","full_name":"Nakanishi, Atsuko"},{"id":"d25163e5-8d53-11eb-a251-e6dd8ea1b8ef","first_name":"Mehmet Orkun","last_name":"Çoruh","orcid":"0000-0002-3219-2022","full_name":"Çoruh, Mehmet Orkun"},{"full_name":"Makino, Fumiaki","last_name":"Makino","first_name":"Fumiaki"},{"last_name":"Miyata","first_name":"Tomoko","full_name":"Miyata, Tomoko"},{"full_name":"Kawamoto, Akihiro","first_name":"Akihiro","last_name":"Kawamoto"},{"first_name":"Ken","last_name":"Yokoyama","full_name":"Yokoyama, Ken"},{"full_name":"Namba, Keiichi","last_name":"Namba","first_name":"Keiichi"},{"first_name":"Genji","last_name":"Kurisu","full_name":"Kurisu, Genji"},{"first_name":"Takayuki","last_name":"Kato","full_name":"Kato, Takayuki"}],"issue":"5","publisher":"Oxford University Press","article_type":"original","page":"249-261","quality_controlled":"1","file_date_updated":"2023-02-03T08:34:48Z","doi":"10.1093/jmicro/dfac037","day":"01","abstract":[{"lang":"eng","text":"Progress in structural membrane biology has been significantly accelerated by the ongoing 'Resolution Revolution' in cryo electron microscopy (cryo-EM). In particular, structure determination by single particle analysis has evolved into the most powerful method for atomic model building of multisubunit membrane protein complexes. This has created an ever increasing demand in cryo-EM machine time, which to satisfy is in need of new and affordable cryo electron microscopes. Here, we review our experience in using the JEOL CRYO ARM 200 prototype for the structure determination by single particle analysis of three different multisubunit membrane complexes: the Thermus thermophilus V-type ATPase VO complex, the Thermosynechococcus elongatus photosystem I monomer and the flagellar motor LP-ring from Salmonella enterica."}],"date_updated":"2023-08-03T12:13:37Z","citation":{"ama":"Gerle C, Kishikawa J, Yamaguchi T, et al. Structures of multisubunit membrane complexes with the CRYO ARM 200. <i>Microscopy</i>. 2022;71(5):249-261. doi:<a href=\"https://doi.org/10.1093/jmicro/dfac037\">10.1093/jmicro/dfac037</a>","apa":"Gerle, C., Kishikawa, J., Yamaguchi, T., Nakanishi, A., Çoruh, M. O., Makino, F., … Kato, T. (2022). Structures of multisubunit membrane complexes with the CRYO ARM 200. <i>Microscopy</i>. Oxford University Press. <a href=\"https://doi.org/10.1093/jmicro/dfac037\">https://doi.org/10.1093/jmicro/dfac037</a>","ieee":"C. Gerle <i>et al.</i>, “Structures of multisubunit membrane complexes with the CRYO ARM 200,” <i>Microscopy</i>, vol. 71, no. 5. Oxford University Press, pp. 249–261, 2022.","chicago":"Gerle, Christoph, Jun-ichi Kishikawa, Tomoko Yamaguchi, Atsuko Nakanishi, Mehmet Orkun Çoruh, Fumiaki Makino, Tomoko Miyata, et al. “Structures of Multisubunit Membrane Complexes with the CRYO ARM 200.” <i>Microscopy</i>. Oxford University Press, 2022. <a href=\"https://doi.org/10.1093/jmicro/dfac037\">https://doi.org/10.1093/jmicro/dfac037</a>.","mla":"Gerle, Christoph, et al. “Structures of Multisubunit Membrane Complexes with the CRYO ARM 200.” <i>Microscopy</i>, vol. 71, no. 5, Oxford University Press, 2022, pp. 249–61, doi:<a href=\"https://doi.org/10.1093/jmicro/dfac037\">10.1093/jmicro/dfac037</a>.","short":"C. Gerle, J. Kishikawa, T. Yamaguchi, A. Nakanishi, M.O. Çoruh, F. Makino, T. Miyata, A. Kawamoto, K. Yokoyama, K. Namba, G. Kurisu, T. Kato, Microscopy 71 (2022) 249–261.","ista":"Gerle C, Kishikawa J, Yamaguchi T, Nakanishi A, Çoruh MO, Makino F, Miyata T, Kawamoto A, Yokoyama K, Namba K, Kurisu G, Kato T. 2022. Structures of multisubunit membrane complexes with the CRYO ARM 200. Microscopy. 71(5), 249–261."},"year":"2022","isi":1,"external_id":{"isi":["000837950900001"],"pmid":["35861182"]},"acknowledgement":"Cyclic Innovation for Clinical Empowerment (JP17pc0101020 from Japan Agency for Medical Research and Development (AMED) to K.N. and G.K.); Platform Project for Supporting Drug Discovery and Life Science Research (Basis for Supporting Innovative Drug Discovery and Life Science Research) from AMED (JP20am0101117 to K.N., JP16K07266 to Atsunori Oshima and C.G., JP22ama121001j0001 to Masaki Yamamoto, G.K., T.K. and C.G.); a JSPS KAHKENHI\r\ngrant (20K06514 to J.K.) and a Grant-in-aid for JSPS fellows (20J00162 to A.N.).\r\nWe are grateful for initiation and scientific support from Matthias Rogner, Marc M. Nowaczyk, Anna Frank and ̈Yuko Misumi for the PSI monomer project and also would like to thank Hideki Shigematsu for critical reading of the manuscript. And we are indebted to the two anonymous reviewers who helped us to improve our manuscript.","volume":71,"ddc":["570"]}]