Laboratory of Supramolecular Crystallography

Member

Director Atsushi NAKAGAWA
Tomitake TSUKIHARA (Guest Professor)
Associate Professor Mamoru SUZUKI
Eiki YAMASHITA
Assistant Professor Mayumi AMANO
Akifumi HIGASHIURA
Hirotaka NARITA

 

Correspondence

Tel 81-6-6879-8635
Fax 81-6-6879-4313
E-mail
URL http://www.protein.osaka-u.ac.jp/rcsfp/supracryst/en

Research

There exist various biological macromolecular assemblies consisting of proteins, nucleic acids, sugars, lipids, and other substances in living cells. These macromolecular assemblies play key roles in all living system. Our laboratory works on structure determination of biological macromolecular assemblies, as well as proteins, which play important roles in biological system, using X-ray crystallography. Development of tools for structure determination of biological macromolecular assemblies, including development and management of the beamline for macromolecular assemblies at SPring-8 (BL44XU), is also one of our main work. Development of Coherent X-ray Diffraction Imaging technique for non-crystalline virus particles is now in progress.

Fig1
Fig.1: Diffraction data collection system installed at the beamline for macromolecular assemblies at SPring-8.
Fig2
Fig. 2: Atomic model of voltage-gated proton channel (VSOP/Hv1)

 

Current Research Programs

  1. X-ray structure determination of macromolecular assemblies and proteins
  2. Development methodologies for X-ray crystal structure determination of biological macromolecular assemblies using synchrotron radiation and X-ray free electron laser
  3. Development of data processing algorithm of diffraction data from micro-crystals

References

  1. X-ray crystal structure of voltage-gated proton channel. Takeshita, K. et al. (2014) Nat. Struct. Mol. Biol., 21, 352-357.
  2. High-resolution X-ray crystal structure of bovine H-protein using the high-pressure cryocooling method. Higashiura, A. et al. (2013) J. Synchrotron Rad., 20, 989-993.
  3. A new protein complex promoting the assembly of Rad51 filaments. Sasanuma, H. et al. (2013) Nat. Commun., 4, 1676.