| Project/Area Number |
10359003
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| Research Category |
Grant-in-Aid for Scientific Research (A).
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| Allocation Type | Single-year Grants |
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| Section | 展開研究 |
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| Research Field |
広領域
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| Research Institution | Nara Institute of Science and Technology |
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Principal Investigator |
HAKOSHIMA Toshio Nara Institute of Science and Technology, Department of Molecular Biology, Professor, バイオサイエンス研究科, 教授 (00164773)
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| Co-Investigator(Kenkyū-buntansha) |
HIGASHI Tsuneyuki Rigaku Co., X-ray Institute, Executive Director, X腺研究所, 部長(研究職)
清水 敏之 奈良先端科学技術大学院大学, バイオサイエンス研究科, 助手 (30273858)
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| Project Period (FY) |
1998 – 2000
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| Project Status |
Completed (Fiscal Year 2000)
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| Budget Amount *help |
¥24,000,000 (Direct Cost: ¥24,000,000)
Fiscal Year 2000: ¥4,300,000 (Direct Cost: ¥4,300,000)
Fiscal Year 1999: ¥8,700,000 (Direct Cost: ¥8,700,000)
Fiscal Year 1998: ¥11,000,000 (Direct Cost: ¥11,000,000)
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| Keywords | transcription / signal transduction / G protein / protein / DNA / molecular complex / X-ray / structural biology / 光学系 / ミラー / イメージングプレート / 構造生物学 |
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| Research Abstract |
An in-house system for X-ray intensity data collection from bio-macromolecular crystals was developed. The system consists of a new X-ray detector(RAXIS-IV)and an improved fine focused(0.1 mm x 1.0 mm)X-ray generator(FR-C). Using two large(300 mm x 300 mm)imaging plates, the detector was designed to yield a short read-out time with high sensitivity. The X-ray beam was focused with Supper's double-mirror. The system was used for data collections of several protein-DNA complex protein-ligand complex and protein-protein crystals and structure determinations of these crystals were performed using the intensity data obtained. These are the mouse transcription factor IRF-2 complexed with DNA, the fission yeast transcription factor Papl complexed with DNA, mouse hippocampal serine protease neuropsin, the human small G protein RhoA in the GTP γS-Mg^<2+> bound form and its complex with the effector protein PKN, and the mouse radixin FERM domain in the free, IP3-bound, and ICAM-2-bound forms.
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