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
Marcel BOKHOVE	Postdoctoral Researcher	mbokhove	3528
Kenichi NISHIKAWA	Staff	nishiken	3356
Fumie OGURA	Technician	fumie	7846
Emi HORIASAKA	Technician	emi.horisaka	3408
Tomoko ISHIHARA	Technician	tomoko.isihara	3919

*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

Suzuki R., Baba S., Mizuno N., Hasegawa K., Koizumi H., Kojima K., Kumasaka T. and Tachibana M.
Radiation-induced defects in protein crystals observed by X-ray topography
Acta Cryst, D78(2): (2022) .
Baba S., Matsuura H., Kawamura T., Sakai N., Nakamura Y., Kawano Y., Mizuno N., Kumasaka T., Yamamoto M. and Hirata K.
Guidelines for de novo phasing using multiple small-wedge data collection
J Synchrotron Radiat,, 28(3):1284-1295 (2021) .
Matsumoto S., Taniguchi-Tamura H., Araki M, Kawamura T, Miyamoto R, Tsuda C, Shima F, Kumasaka T, Okuno Y and Kataoka T.
Oncogenic mutations Q61L and Q61H confer active form-like structural features to the inactive state (state 1) conformation of H-Ras protein
Biochem Biophys Res Commun, 565:85-90 (2021) .
Nomura T, Kimura T, Kanematsu Y, Yamada D, Yamashita K, Hirata K, Ueno G, Murakami H, Hisano T, Yamagiwa R, Takeda H, Gopalasingam C, Kousaka R, Yanagisawa S, Shoji O, Kumasaka T, Yamamoto M, Takano Y, Sugimoto H, Tosha T, Kubo M and Shiro Y.
Short-lived intermediate in N₂O generation by P450 NO reductase captured by time-resolved IR spectroscopy and XFEL crystallography
Proc Natl Acad Sci USA, 118(21):e2101481118 (2021).
Hattori S, Higashi-Kuwata N, Hayashi H, Allu S, Raghavaiah J, Bulut H, Das D, Anson B, Lendy E, Takamatsu Y, Takamune N, Kishimoto N, Murayama K, Hasegawa K, Li M, Davis D, Kodama E, Yarchoan R, Wlodawer A, Misumi S, Mesecar A, Ghosh A and Mitsuya H
A small molecule compound with an indole moiety inhibits the main protease of SARS-CoV-2 and blocks virus replication
Nat Commun, 12:668 (2021).

> 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.