Studies of a mechanism in stabilizing the redox states of an iron-sulfur protein.
Project/Area Number |
25891030
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Research Category |
Grant-in-Aid for Research Activity Start-up
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Allocation Type | Single-year Grants |
Research Field |
Structural biochemistry
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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)
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Project Period (FY) |
2013-08-30 – 2015-03-31
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Project Status |
Completed (Fiscal Year 2014)
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Budget Amount *help |
¥2,730,000 (Direct Cost: ¥2,100,000、Indirect Cost: ¥630,000)
Fiscal Year 2014: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2013: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
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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.
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Report
(3 results)
Research Products
(6 results)
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[Presentation] 電子伝達タンパク質の中性子構造解析2014
Author(s)
平野優、栗原和男、玉田太郎、日下勝弘、三木邦夫
Organizer
日本中性子科学会第14回年会
Place of Presentation
北海道立道民活動センター「かでる2・7」、札幌
Year and Date
2014-12-11 – 2014-12-12
Related Report
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