Studies of a mechanism in stabilizing the redox states of an iron-sulfur protein.

2014 Fiscal Year Final Research Report

• Project/Area Number: 25891030
• Research Category: Grant-in-Aid for Research Activity Start-up
• Allocation Type: Single-year Grants
• Research Field: Structural biochemistry
• Research Institution: Japan Atomic Energy Agency
• Principal Investigator: HIRANO Yu 独立行政法人日本原子力研究開発機構, 原子力科学研究部門 量子ビーム応用研究センター, 博士研究員 (80710772)
• Project Period (FY): 2013-08-30 – 2015-03-31
• Keywords: 蛋白質 / 中性子構造

Outline of Final Research Achievements

Large crystals were obtained for the oxidized form of high-potential iron-sulfur protein. Neutron diffraction experiment was carried out at the beamline for life science (iBIX) of Japan Proton Accelerator Reseach complex J-PARC. A neutron diffraction data set was collected up to 1.1 angstrom resolution that is the highest resolution in the neutron diffraction data of proteins. After structure refinement, structures of hydrogen atoms were determined for ionizable amino acids and water molecules on the surface of the iron-sulfur protein. In addition, many deviations form ideal values were observed in the structure refinement by relaxing the restraints for bond angles and lengths of hydrogen atoms.

Free Research Field

蛋白質結晶学