SPring-8 Structural Biology Beamlines

Division Information

Member

Japan Synchrotron Radiation Research Institute
Structural Biology Division

Name		e-mail *	PHS
Takashi KUMASAKA	Director	kumasaka	63475
Experimental Instrumentation Team
Kazuya HASEGAWA	Team Leader	kazuya	63595
Seiki BABA	Scientist	baba	63510
Nobuhiro MIZUNO	Scientist	nmizuno	63797
Hideo OKUMURA	Scientist	okumurah	63755
Naomine YANO	Scientist	naomine.yano	63444
Hironori MURAKAMI	Engineer	hiromura	63364
Takuya MASUNAGA	Engineer	takuya.masunaga	63228
Integrated Structural Analysis Team
Naoki SAKAI	Team Leader	nsakai	63838
Hideki SHIGEMATSU	Scientist	shigematsu	67868
Takashi KAWAMURA	Scientist	kawamura	63396
Yuki NAKAMURA	Engineer	y-nakamu	63362
Fumie OGURA	Engineer	fumie	67846
Kenichi NISHIKAWA	Staff(concurrent)	nishiken	63356

*followed by @spring8.or.jp.
Please see here for the Research Project Division (Life Science and Drug Discovery Group).

Activities description

The Structural Biology 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

Nagao S., Kuwano W., Tosha T., Yamashita K., Stanfield J. K., Kasai C., Ariyasu S., Hirata K., Ueno G., Murakami H., Ago H., Yamamoto M., Shoji O., Sugimoto H., Kubo M.
XFEL crystallography reveals catalytic cycle dynamics during non-native substrate oxidation by cytochrome P450BM3
Commun Chem, 8: 63 (2025) .
Hayashi H., Hasegawa K., Saijo R., Kodama E. N., Murayama K.
Binding of a potential antibacterial drug, mangiferin, to serine hydroxymethyltransferase from Enterococcus faecium
Biochem Biophys Res Commun, 743: 151177 (2025) .
Higashi-Kuwata N., Bulut H., Hayashi H., Tsuji K., Ogata-Aoki H., Kiso M., Takamune N., Kishimoto N., Hattori S., Ishii T., Kobayakawa T., Nakano K., Shimizu Y., Das D., Saruwatari J., Hasegawa K., Murayama K., Sukenaga Y., Takamatsu S., Yoshimura K., Aoki M., Furusawa Y., Okamura T., Yamayoshi S., Kawaoka Y., Misumi S., Tamamura H., Mitsuya H.
An orally available P1′-5-fluorinated M^pro inhibitor blocks SARS-CoV-2 replication without booster and exhibits high genetic barrier
PNAS Nexus, 4: pgae578 (2025) .
Hayashi H., Saijo E., Hirata K., Murakami S., Okuda H., Kodama E. N., Hasegawa K., Murayama K.
SHIN-2 exerts potent activity against VanA-type vancomycin-resistant Enterococcus faecium in vitro by stabilizing the active site loop of serine hydroxymethyltransferase
Arch Biochem Biophys, 761: 110160 (2024) .
Abe K., McDermott J., Madapally H. V., Marimuthu P., Gopalasingam C. C., Gerle C., Shigematsu H., Khandelia H., Blanco G.
Molecular Structure of the Na⁺,K⁺-ATPase α4β1 Isoform in Its Ouabain-Bound Conformation
Int. J. Mol. Sci., 25: 12397 (2024) .

> 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.