---
_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. 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
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.
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.
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.
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. 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'
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.'
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.'
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.”
Solid State Nuclear Magnetic Resonance, vol. 87, no. 10, Elsevier, 2017,
pp. 86–95, doi:10.1016/j.ssnmr.2017.04.002.'
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'
...