Research Group:
Synchrotron Structural Biology
Contact:
| Genji Kurisu |
| Institute for Protein Research, Osaka Univ., 3-2 Yamadaoka, Suita, Osaka |
| Telephone: +81-6-6879-8604 |
| gkurisu (at) protein.osaka-u.ac.jp |
Research Area:
Life Science
Beamline:
BL12B2, BL26B1, BL32XU, BL38B1, BL41XU, BL44XU, BL45XU
Overview of Research Group, Goals and Purposes:
The understanding of biological function derived from three-dimensional structures of key proteins and nucleic acids is particularly important in life science and becomes essential for applied biosciences, protein engineering or structure-based drug design. Most of the structure models deposited in the Protein Data Bank (PDB) are determined by macromolecular crystallography (MX) taking advantage of powerful synchrotron radiation (SR). Even though MX is a important tool for this purpose, integrative structural biology (ISB) using multiple techniques such as SAXS, XAFS, CryoTEM and NMR becomes now widespread for better understanding of biological macromolecules.
Even though we can now determine many protein structures very rapidly, we still have difficult-to-solve crystal structures by the issues of large unit cell, small crystal size, poor diffraction quality or severe radiation damage. Therefore, the structural biology beamlines in SR provide a wide range of performance covering the variety of samples with different properties. In SPring-8, there are several characteristic beamlines individually optimized for specific purpose. They are operated not only by JASRI, but also by RIKEN SPring-8 Center and Osaka University. SPring-8 users of structural biology also come from the various organizations of industry, government and academia.
In order to utilize these beamlines more effectively, a national project “Basis for Supporting Innovative Drug Discovery and Life Science Research (BINDS)” is being conducted since 2017, and supports development of ISB. In particular, the significantly progressing CryoTEM technique is being the phase for its public use. Further, serial femtosecond crystallography (SFX) using XFEL/SACLA has given fruitfull results, and then needs to expand its applicability in the framework of ISB. The new SR facility designs, Tohoku and SPring-8, and automatic measurement and remote beamline operation in MX is dynamically and excitingly changing the situation in structural biology. The most important goal of our group is to further develop synchrotron structural biology by supporting the connection between the SPring-8 and the user community.