TY - JOUR
T1 - High-resolution cryo-EM structure of photosystem II reveals damage from high-dose electron beams
AU - Kato, Koji
AU - Miyazaki, Naoyuki
AU - Hamaguchi, Tasuku
AU - Nakajima, Yoshiki
AU - Akita, Fusamichi
AU - Yonekura, Koji
AU - Shen, Jian Ren
N1 - Funding Information:
We thank Keisuke Kawakami for the critical reading of the manuscript. This work was supported by JSPS KAKENHI No. JP20H02914 (K.K.), JP19K22396, JP20H03194 (F.A.), JP20H05087 (N.M.), JP17H06434 (J.-R.S.), JST PRESTO No. JPMJPR16P1 (F.A.), the Platform Project for Supporting Drug Discovery and Life Science Research (Basis for Supporting Innovative Drug Discovery, Life Science Research (BINDS)) of AMED No. JP18am0101072j002 (N.M.), and the Cyclic Innovation for Clinical Empowerment (CiCLE) from AMED and the JST-Mirai Program Grant Number JPMJMI20G5 (K.Y.).
Publisher Copyright:
© 2021, The Author(s).
PY - 2021/12
Y1 - 2021/12
N2 - Photosystem II (PSII) plays a key role in water-splitting and oxygen evolution. X-ray crystallography has revealed its atomic structure and some intermediate structures. However, these structures are in the crystalline state and its final state structure has not been solved. Here we analyzed the structure of PSII in solution at 1.95 Å resolution by single-particle cryo-electron microscopy (cryo-EM). The structure obtained is similar to the crystal structure, but a PsbY subunit was visible in the cryo-EM structure, indicating that it represents its physiological state more closely. Electron beam damage was observed at a high-dose in the regions that were easily affected by redox states, and reducing the beam dosage by reducing frames from 50 to 2 yielded a similar resolution but reduced the damage remarkably. This study will serve as a good indicator for determining damage-free cryo-EM structures of not only PSII but also all biological samples, especially redox-active metalloproteins.
AB - Photosystem II (PSII) plays a key role in water-splitting and oxygen evolution. X-ray crystallography has revealed its atomic structure and some intermediate structures. However, these structures are in the crystalline state and its final state structure has not been solved. Here we analyzed the structure of PSII in solution at 1.95 Å resolution by single-particle cryo-electron microscopy (cryo-EM). The structure obtained is similar to the crystal structure, but a PsbY subunit was visible in the cryo-EM structure, indicating that it represents its physiological state more closely. Electron beam damage was observed at a high-dose in the regions that were easily affected by redox states, and reducing the beam dosage by reducing frames from 50 to 2 yielded a similar resolution but reduced the damage remarkably. This study will serve as a good indicator for determining damage-free cryo-EM structures of not only PSII but also all biological samples, especially redox-active metalloproteins.
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U2 - 10.1038/s42003-021-01919-3
DO - 10.1038/s42003-021-01919-3
M3 - Article
C2 - 33753866
AN - SCOPUS:85103199008
SN - 2399-3642
VL - 4
JO - Communications Biology
JF - Communications Biology
IS - 1
M1 - 382
ER -
