[{"title":"Structures of multisubunit membrane complexes with the CRYO ARM 200","author":[{"first_name":"Christoph","last_name":"Gerle","full_name":"Gerle, Christoph"},{"full_name":"Kishikawa, Jun-ichi","last_name":"Kishikawa","first_name":"Jun-ichi"},{"first_name":"Tomoko","full_name":"Yamaguchi, Tomoko","last_name":"Yamaguchi"},{"last_name":"Nakanishi","full_name":"Nakanishi, Atsuko","first_name":"Atsuko"},{"first_name":"Mehmet Orkun","id":"d25163e5-8d53-11eb-a251-e6dd8ea1b8ef","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","full_name":"Miyata, Tomoko","first_name":"Tomoko"},{"last_name":"Kawamoto","full_name":"Kawamoto, Akihiro","first_name":"Akihiro"},{"first_name":"Ken","full_name":"Yokoyama, Ken","last_name":"Yokoyama"},{"full_name":"Namba, Keiichi","last_name":"Namba","first_name":"Keiichi"},{"first_name":"Genji","full_name":"Kurisu, Genji","last_name":"Kurisu"},{"last_name":"Kato","full_name":"Kato, Takayuki","first_name":"Takayuki"}],"article_processing_charge":"No","external_id":{"pmid":["35861182"],"isi":["000837950900001"]},"user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","citation":{"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.” Microscopy. Oxford University Press, 2022. https://doi.org/10.1093/jmicro/dfac037.","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.","mla":"Gerle, Christoph, et al. “Structures of Multisubunit Membrane Complexes with the CRYO ARM 200.” Microscopy, vol. 71, no. 5, Oxford University Press, 2022, pp. 249–61, doi:10.1093/jmicro/dfac037.","ama":"Gerle C, Kishikawa J, Yamaguchi T, et al. Structures of multisubunit membrane complexes with the CRYO ARM 200. Microscopy. 2022;71(5):249-261. doi:10.1093/jmicro/dfac037","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. Microscopy. Oxford University Press. https://doi.org/10.1093/jmicro/dfac037","ieee":"C. Gerle et al., “Structures of multisubunit membrane complexes with the CRYO ARM 200,” Microscopy, vol. 71, no. 5. Oxford University Press, pp. 249–261, 2022.","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."},"quality_controlled":"1","publisher":"Oxford University Press","oa":1,"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.","doi":"10.1093/jmicro/dfac037","date_published":"2022-10-01T00:00:00Z","date_created":"2022-07-25T10:04:58Z","page":"249-261","day":"01","publication":"Microscopy","isi":1,"has_accepted_license":"1","year":"2022","status":"public","keyword":["Radiology","Nuclear Medicine and imaging","Instrumentation","Structural Biology"],"type":"journal_article","article_type":"original","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)","short":"CC BY (4.0)"},"_id":"11648","department":[{"_id":"LeSa"}],"file_date_updated":"2023-02-03T08:34:48Z","ddc":["570"],"date_updated":"2023-08-03T12:13:37Z","month":"10","intvolume":" 71","scopus_import":"1","oa_version":"Published Version","pmid":1,"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."}],"issue":"5","volume":71,"file":[{"creator":"dernst","file_size":7812696,"date_updated":"2023-02-03T08:34:48Z","file_name":"2022_Microscopy_Gerle.pdf","date_created":"2023-02-03T08:34:48Z","relation":"main_file","access_level":"open_access","content_type":"application/pdf","success":1,"checksum":"23b51c163636bf9313f7f0818312e67e","file_id":"12498"}],"language":[{"iso":"eng"}],"publication_identifier":{"eissn":["2050-5701"],"issn":["2050-5698"]},"publication_status":"published"},{"abstract":[{"text":"Solid-state NMR spectroscopy can provide site-resolved information about protein dynamics over many time scales. Here we combine protein deuteration, fast magic-angle spinning (~45–60 kHz) and proton detection to study dynamics of ubiquitin in microcrystals, and in particular a mutant in a region that undergoes microsecond motions in a β-turn region in the wild-type protein. We use 15N R1ρ relaxation measurements as a function of the radio-frequency (RF) field strength, i.e. relaxation dispersion, to probe how the G53A mutation alters these dynamics. We report a population-inversion of conformational states: the conformation that in the wild-type protein is populated only sparsely becomes the predominant state. We furthermore explore the potential to use amide-1H R1ρ relaxation to obtain insight into dynamics. We show that while quantitative interpretation of 1H relaxation remains beyond reach under the experimental conditions, due to coherent contributions to decay, one may extract qualitative information about flexibility.","lang":"eng"}],"oa_version":"None","publisher":"Elsevier","quality_controlled":"1","intvolume":" 87","month":"10","publication_status":"published","year":"2017","publication_identifier":{"issn":["0926-2040"]},"publication":"Solid State Nuclear Magnetic Resonance","language":[{"iso":"eng"}],"day":"01","page":"86-95","date_created":"2020-09-18T10:06:18Z","volume":87,"issue":"10","doi":"10.1016/j.ssnmr.2017.04.002","date_published":"2017-10-01T00:00:00Z","_id":"8447","type":"journal_article","article_type":"original","keyword":["Nuclear and High Energy Physics","Instrumentation","General Chemistry","Radiation"],"status":"public","date_updated":"2021-01-12T08:19:20Z","citation":{"ama":"Gauto DF, Hessel A, Rovó P, Kurauskas V, Linser R, Schanda P. Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals. Solid State Nuclear Magnetic Resonance. 2017;87(10):86-95. doi:10.1016/j.ssnmr.2017.04.002","apa":"Gauto, D. F., Hessel, A., Rovó, P., Kurauskas, V., Linser, R., & Schanda, P. (2017). Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals. Solid State Nuclear Magnetic Resonance. Elsevier. https://doi.org/10.1016/j.ssnmr.2017.04.002","ieee":"D. F. Gauto, A. Hessel, P. Rovó, V. Kurauskas, R. Linser, and P. Schanda, “Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals,” Solid State Nuclear Magnetic Resonance, vol. 87, no. 10. Elsevier, pp. 86–95, 2017.","short":"D.F. Gauto, A. Hessel, P. Rovó, V. Kurauskas, R. Linser, P. Schanda, Solid State Nuclear Magnetic Resonance 87 (2017) 86–95.","mla":"Gauto, Diego F., et al. “Protein Conformational Dynamics Studied by 15N and 1HR1ρ Relaxation Dispersion: Application to Wild-Type and G53A Ubiquitin Crystals.” Solid State Nuclear Magnetic Resonance, vol. 87, no. 10, Elsevier, 2017, pp. 86–95, doi:10.1016/j.ssnmr.2017.04.002.","ista":"Gauto DF, Hessel A, Rovó P, Kurauskas V, Linser R, Schanda P. 2017. Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals. Solid State Nuclear Magnetic Resonance. 87(10), 86–95.","chicago":"Gauto, Diego F., Audrey Hessel, Petra Rovó, Vilius Kurauskas, Rasmus Linser, and Paul Schanda. “Protein Conformational Dynamics Studied by 15N and 1HR1ρ Relaxation Dispersion: Application to Wild-Type and G53A Ubiquitin Crystals.” Solid State Nuclear Magnetic Resonance. Elsevier, 2017. https://doi.org/10.1016/j.ssnmr.2017.04.002."},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","extern":"1","article_processing_charge":"No","author":[{"last_name":"Gauto","full_name":"Gauto, Diego F.","first_name":"Diego F."},{"last_name":"Hessel","full_name":"Hessel, Audrey","first_name":"Audrey"},{"full_name":"Rovó, Petra","last_name":"Rovó","first_name":"Petra"},{"first_name":"Vilius","last_name":"Kurauskas","full_name":"Kurauskas, Vilius"},{"last_name":"Linser","full_name":"Linser, Rasmus","first_name":"Rasmus"},{"orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul"}],"title":"Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion: Application to wild-type and G53A ubiquitin crystals"}]