Life Science Group

Group Leader: SENDA, Toshiya

Our group promotes research in the field of life science using synchrotron radiation, for which we have developed state-of-the-art beamlines and experimental devices. We have expanded our research to link biopolymers to cells and tissues using X-ray crystal structural analysis, small-angle X-ray scattering, X-ray imaging, and X-ray cell irradiation.

In addition to the research by the department staff, our school promotes interuniversity research as one of the interuniversity research institutes. We also conduct research in cooperation with industry, academia, and the government in the fields of pharmacy, nutrition, and the environment.

[Main Research Projects]

Elucidation of functions and mechanisms of nuclear proteins in eukaryotes
Mechanism that disassembles a particular part of a nucleosome in a chromosome to activate a gene.

We are studying the intranuclear reactions in a cell, such as transcription and replication from a chromatin template, using the spatial structures of biopolymers such as proteins, DNA, and RNA. In particular, with a focus on the relationship between epigenetic information and intranuclear reactions, we are studying how the functions of individual molecules integrate to yield complex functions.

Elucidation of the causes of diseases determined from the structures of proteins related to infectious and other diseases

We are studying the causes of infection and diseases by studying the spatial structures of molecules (molecular complex) related to infectious and other diseases, and we aim to establish the foundation for the discovery of drugs to fight these diseases.

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Mechanism that disrupts the intracellular signals by the protein CagA in Helicobacter pylori (left), and the crystal structure of CagA (right).
Elucidation of the mechanisms of enzyme reactions

We are studying the spatial structures of intermediate enzymes to elucidate the relationship between the spatial structures and the functions of enzymes that help chemical reactions in a living body.

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Entire structure of the PCB decomposition enzyme BphC (left), and the structure of the active center (right).
Elucidation of the mechanism of intracellular and extracellular signaling and substance transportation
Schematic diagram of intracellular transportation
(by Professor Yoshimori at Osaka University).

We are studying the structure of biopolymers (biopolymer complex) to elucidate the mechanisms of intracellular and extracellular signaling and substance transportation.

Elucidation of the mechanism of biological effects of radiation
The nuclei of human cells (red) irradiated with a 5-μm beam (in the frame on the right), and damaged DNA parts (green).

We are studying the effects of radiation on cells, from the molecular level to the tissue level, by using the variable energy of synchrotron radiation and microbeams obtained from highly-collimated X-rays.

Development of a synchrotron radiation X-ray imaging system that can be applied to medical science
Phase image (a) and absorption image
(b) of a slice of the cerebellum of a rat.

To obtain knowledge from imaging data about a living body and various diseases, we are developing an imaging system that utilizes the characteristics of synchrotron radiation, and conducting research into its application.

Development of advanced methods and devices for synchrotron radiation research in life science

Device for protein crystal structural analysis; it includes a large-area detector, a highly accurate axis of rotation, and a crystal exchange robot.

We are upgrading to new analysis methods and beamlines, and developing multifaceted analysis methods by combining multiple methods. We will provide these methods for joint usage.


Organization of the Photon Factory

[Beamlines in Charge]

Macromolecular crystallography

BL-1A, BL-5A, BL-17A, NE-3A, NW-12A

Small-angle X-ray scattering of muscle and alloys

BL-6A, BL-10C, BL-15A2

X-ray imaging and multi-purpose experiments

BL-14C, (NE-5A), NE-7A

Radiation biology, microbeam irradiation system

BL-27A, BL-27B


Structural Biology Research Center