SPring-8 Structural Biology Beamlines

Division Information

Member

Japan Synchrotron Radiation Research Institute
Protein Crystal Analysis Division

Name		e-mail *	PHS
Takashi KUMASAKA	Director	kumasaka	3475
Naoto YAGI	Coordinator	yagi	3852
Kazuya HASEGAWA	Team Leader	kazuya	3595
Seiki BABA	Scientist	baba	3510
Nobuhiro MIZUNO	Scientist	nmizuno	3797
Hideo OKUMURA	Scientist	okumurah	3755
Hironori MURAKAMI	Engineer	hiromura	3364
Yuki NAKAMURA	Engineer	y-nakamu	3362
Takuya MASUNAGA	Engineer	takuya.masunaga	3228
Takashi KAWAMURA	Scientist	kawamura	3396
Makoto NAKABAYASHI	Scientist	makoto-n	3875
Kenichi NISHIKAWA	Staff	nishiken	3356
Aimi OSAKI	Technician	aimi	3487
Fumie OGURA	Technician	fumie	7846

*followed by @spring8.or.jp.

Activities description

The Protein Crystal Analysis Division is mainly responsible for the development and maintenance of the research environment for structural biology using the high-brilliance synchrotron radiation at SPring-8. Our Division also develops the advanced research environment to promote structural biology research aimed at elucidating biological systems.
We support academic research by maintaining and upgrading the public beamlines, Structural Biology I (BL41XU: Undulator) and Structural Biology III (BL45XU: Undulator).
In addition, in order to meet the increasing needs of users and to promote the use of the beamline, we are upgrading the following items,

(1) Development of methods to automate and remotely use experiments to speed up structural decisions
(2) Development of instruments aimed at application to samples that are difficult to analyze in the past (e.g., microcrystals and ultra-high resolution structure determination)

In addition, we are conducting crystal structure analysis of proteins, metalloproteins, and viruses in the cellular signaling system as a group to advance structural biology research and develop advanced analysis methods.

Publications

Ohnishi Y, Muraki N, Kiyota D, Okumura H, Baba S, Kawano Y, Kumasaka T, Tanaka H, Kurisu G.
X-ray dose-dependent structural changes of the [2Fe-2S] ferredoxin from Chlamydomonas einhardtii.
J Biochem., (2020) [doi: 10.1093/jb/mvaa045].
Murakami H, Hasegawa K, Ueno G, Yagi N, Yamamoto M and Kumasaka T.
Development of SPACE-II for rapid sample exchange at SPring-8 macromolecular crystallography beamlines.
Acta Cryst. D, 76(2):155-165 (2020).
Suga M, Akita F, Yamashita K, Nakajima Y, Ueno G, Li H, Yamane T, Umena Y, Yonekura S, Yu LJ, Murakami H, Nomura T, Kimura T, Kubo M, Baba S, Kumasaka T, Tono K, Yabashi M, Isobe H, Yamaguchi K, Yamamoto M, Ago H and, Shen JR.
An oxyl/oxo mechanism for oxygen-oxygen coupling in PSII revealed by an x-ray free-electron laser.
Science, 366(6463):334-338 (2019).
Baba S, Shimada A, Mizuno N, Baba J, Ago H, Yamamoto M and Kumasaka T.
A temperature-controlled cold-gas humidifier and its application to protein crystals with the humid-air and glue-coating method.
J Appl Cryst, 52(4):699-705 (2019).
Ueno G, Shimada A, Yamashita E, Hasegawa K, Kumasaka T, Shinzawa-Itoh K, Yoshikawa S, Tsukihara T and Yamamoto M.
Low-dose X-ray structure analysis of cytochrome c oxidase utilizing high-energy X-rays.
J Synchrotron Radiat, 26(4):912-921 (2019).

> Publications View

We are developing and improving the structural biology research environment using the high-brilliance synchrotron radiation at SPring-8.

Division Information

Member

Activities description

Publications

We are developing and improving the structural biology research environment
using the high-brilliance synchrotron radiation at SPring-8.