---
_id: '11648'
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.'
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."
article_processing_charge: No
article_type: original
author:
- first_name: Christoph
  full_name: Gerle, Christoph
  last_name: Gerle
- first_name: Jun-ichi
  full_name: Kishikawa, Jun-ichi
  last_name: Kishikawa
- first_name: Tomoko
  full_name: Yamaguchi, Tomoko
  last_name: Yamaguchi
- first_name: Atsuko
  full_name: Nakanishi, Atsuko
  last_name: Nakanishi
- first_name: Mehmet Orkun
  full_name: Çoruh, Mehmet Orkun
  id: d25163e5-8d53-11eb-a251-e6dd8ea1b8ef
  last_name: Çoruh
  orcid: 0000-0002-3219-2022
- first_name: Fumiaki
  full_name: Makino, Fumiaki
  last_name: Makino
- first_name: Tomoko
  full_name: Miyata, Tomoko
  last_name: Miyata
- first_name: Akihiro
  full_name: Kawamoto, Akihiro
  last_name: Kawamoto
- first_name: Ken
  full_name: Yokoyama, Ken
  last_name: Yokoyama
- first_name: Keiichi
  full_name: Namba, Keiichi
  last_name: Namba
- first_name: Genji
  full_name: Kurisu, Genji
  last_name: Kurisu
- first_name: Takayuki
  full_name: Kato, Takayuki
  last_name: Kato
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>
  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>.
  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.
  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.” <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.
date_created: 2022-07-25T10:04:58Z
date_published: 2022-10-01T00:00:00Z
date_updated: 2023-08-03T12:13:37Z
day: '01'
ddc:
- '570'
department:
- _id: LeSa
doi: 10.1093/jmicro/dfac037
external_id:
  isi:
  - '000837950900001'
  pmid:
  - '35861182'
file:
- access_level: open_access
  checksum: 23b51c163636bf9313f7f0818312e67e
  content_type: application/pdf
  creator: dernst
  date_created: 2023-02-03T08:34:48Z
  date_updated: 2023-02-03T08:34:48Z
  file_id: '12498'
  file_name: 2022_Microscopy_Gerle.pdf
  file_size: 7812696
  relation: main_file
  success: 1
file_date_updated: 2023-02-03T08:34:48Z
has_accepted_license: '1'
intvolume: '        71'
isi: 1
issue: '5'
keyword:
- Radiology
- Nuclear Medicine and imaging
- Instrumentation
- Structural Biology
language:
- iso: eng
month: '10'
oa: 1
oa_version: Published Version
page: 249-261
pmid: 1
publication: Microscopy
publication_identifier:
  eissn:
  - 2050-5701
  issn:
  - 2050-5698
publication_status: published
publisher: Oxford University Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Structures of multisubunit membrane complexes with the CRYO ARM 200
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 71
year: '2022'
...
---
_id: '8447'
abstract:
- lang: eng
  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.'
article_processing_charge: No
article_type: original
author:
- first_name: Diego F.
  full_name: Gauto, Diego F.
  last_name: Gauto
- first_name: Audrey
  full_name: Hessel, Audrey
  last_name: Hessel
- first_name: Petra
  full_name: Rovó, Petra
  last_name: Rovó
- first_name: Vilius
  full_name: Kurauskas, Vilius
  last_name: Kurauskas
- first_name: Rasmus
  full_name: Linser, Rasmus
  last_name: Linser
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
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. <i>Solid State Nuclear Magnetic Resonance</i>. 2017;87(10):86-95.
    doi:<a href="https://doi.org/10.1016/j.ssnmr.2017.04.002">10.1016/j.ssnmr.2017.04.002</a>'
  apa: 'Gauto, D. F., Hessel, A., Rovó, P., Kurauskas, V., Linser, R., &#38; Schanda,
    P. (2017). Protein conformational dynamics studied by 15N and 1HR1ρ relaxation
    dispersion: Application to wild-type and G53A ubiquitin crystals. <i>Solid State
    Nuclear Magnetic Resonance</i>. Elsevier. <a href="https://doi.org/10.1016/j.ssnmr.2017.04.002">https://doi.org/10.1016/j.ssnmr.2017.04.002</a>'
  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.” <i>Solid State
    Nuclear Magnetic Resonance</i>. Elsevier, 2017. <a href="https://doi.org/10.1016/j.ssnmr.2017.04.002">https://doi.org/10.1016/j.ssnmr.2017.04.002</a>.'
  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,” <i>Solid State Nuclear
    Magnetic Resonance</i>, vol. 87, no. 10. Elsevier, pp. 86–95, 2017.'
  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.'
  mla: 'Gauto, Diego F., et al. “Protein Conformational Dynamics Studied by 15N and
    1HR1ρ Relaxation Dispersion: Application to Wild-Type and G53A Ubiquitin Crystals.”
    <i>Solid State Nuclear Magnetic Resonance</i>, vol. 87, no. 10, Elsevier, 2017,
    pp. 86–95, doi:<a href="https://doi.org/10.1016/j.ssnmr.2017.04.002">10.1016/j.ssnmr.2017.04.002</a>.'
  short: D.F. Gauto, A. Hessel, P. Rovó, V. Kurauskas, R. Linser, P. Schanda, Solid
    State Nuclear Magnetic Resonance 87 (2017) 86–95.
date_created: 2020-09-18T10:06:18Z
date_published: 2017-10-01T00:00:00Z
date_updated: 2021-01-12T08:19:20Z
day: '01'
doi: 10.1016/j.ssnmr.2017.04.002
extern: '1'
intvolume: '        87'
issue: '10'
keyword:
- Nuclear and High Energy Physics
- Instrumentation
- General Chemistry
- Radiation
language:
- iso: eng
month: '10'
oa_version: None
page: 86-95
publication: Solid State Nuclear Magnetic Resonance
publication_identifier:
  issn:
  - 0926-2040
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: 'Protein conformational dynamics studied by 15N and 1HR1ρ relaxation dispersion:
  Application to wild-type and G53A ubiquitin crystals'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 87
year: '2017'
...