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Suga, Michihiro Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University ORCID Kaken ID researchmap
Shimada, Atsuhiro Graduate School of Applied Biological Sciences and Faculty of Applied Biological Sciences, Gifu University
Akita, Fusamichi Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University ORCID Kaken ID publons researchmap
Shen, Jian-Ren Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University ORCID Kaken ID publons researchmap
Tosha, Takehiko Synchrotron Radiation Life Science Instrumentation Team, RIKEN SPring-8 Center
Sugimoto, Hiroshi Synchrotron Radiation Life Science Instrumentation Team, RIKEN SPring-8 Center
Background: The invention of the X-ray free-electron laser (XFEL) has provided unprecedented new opportunities for structural biology. The advantage of XFEL is an intense pulse of X-rays and a very short pulse duration (<10 fs) promising a damage-free and time-resolved crystallography approach.
Scope of review: Recent time-resolved crystallographic analyses in XFEL facility SACLA are reviewed. Specifically, metalloproteins involved in the essential reactions of bioenergy conversion including photosystem II, cytochrome c oxidase and nitric oxide reductase are described.
Major conclusions: XFEL with pump-probe techniques successfully visualized the process of the reaction and the dynamics of a protein. Since the active center of metalloproteins is very sensitive to the X-ray radiation, damage-free structures obtained by XFEL are essential to draw mechanistic conclusions. Methods and tools for sample delivery and reaction initiation are key for successful measurement of the time-resolved data.
General significance: XFEL is at the center of approaches to gain insight into complex mechanism of structural dynamics and the reactions catalyzed by biological macromolecules. Further development has been carried out to expand the application of time-resolved X-ray crystallography. This article is part of a Special Issue entitled Novel measurement techniques for visualizing 'live' protein molecules.
Serial femtosecond crystallography
X-ray free-electron laser
Biochimica et Biophysica Acta (BBA) - General Subjects
© 2019 The Author(s). Published by Elsevier B.V.
|Web of Science KeyUT|
Michihiro Suga, Atsuhiro Shimada, Fusamichi Akita, Jian-Ren Shen, Takehiko Tosha, Hiroshi Sugimoto, Time-resolved studies of metalloproteins using X-ray free electron laser radiation at SACLA, Biochimica et Biophysica Acta (BBA) - General Subjects, Volume 1864, Issue 2, 2020, 129466, ISSN 0304-4165, https://doi.org/10.1016/j.bbagen.2019.129466.
Japan Society for the Promotion of Science
|Open Access (Publisher)||
|Open Archive (publisher)||