| Project/Area Number |
04404088
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| Research Category |
Grant-in-Aid for General Scientific Research (A)
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| Allocation Type | Single-year Grants |
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| Research Field |
結晶学
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| Research Institution | Nagaoka University of Thchnology |
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Principal Investigator |
MITSUI Yukio Nagaoka University of Technology Faculty of Engineering, Professor, 工学部, 教授 (40012637)
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| Co-Investigator(Kenkyū-buntansha) |
KAWANO Genji Toray Industries Inc., Institute for Biomedical Research, Pricipal Investigator, 医療システム研究所, 主席研究員
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| Project Period (FY) |
1992 – 1994
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| Project Status |
Completed (Fiscal Year 1994)
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| Budget Amount *help |
¥22,000,000 (Direct Cost: ¥22,000,000)
Fiscal Year 1994: ¥3,000,000 (Direct Cost: ¥3,000,000)
Fiscal Year 1993: ¥5,000,000 (Direct Cost: ¥5,000,000)
Fiscal Year 1992: ¥14,000,000 (Direct Cost: ¥14,000,000)
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| Keywords | Two-dimensional X-ray diffractometer / Protein crystallography / Cytokine / Interferon / X-ray crystal structure analysis / Protein engineering / Structure-activity relationship / 構造-活性相関 / X線回折計 / 結晶化 / コンピューターグラフィックス |
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| Research Abstract |
1) Set-up of the X-ray diffractometer system.
The "recording device for diffracted X-ray beam", whcih was purchased by the present grant, completed the set-up of the two-dimensional X-ray diffraactometer using Imaging Plates.
2) Set-up of the computer graphics system.
The "CPU-upgrading system" purchased by the present grant, was succesfully incorporated into the existing system extensively upgrading its performance.
3) Refinement of the crystal structure of murine interferon-beta
Using the systems 1) and 2) above, the structure has been refined at 2.15 A resolution to an R-factor of 19.1%. Extensive modification was found necessary for the A-Helix portion (EMBO Journal 4,3193-3201 (1993) ; also submitted to J.Mol.Biol.)
4) Prediction of the three-dimensional structures for various Type I interferons.
Structure prediction was done for the following four interferons : human-alphaD,human-beta, bovine & ovine tau's. A huge data set of the structure-activity relationship studiesdirected for Type I interferons were compiled and systematically evaluated based on the established three-dimensional structure(Pharmacology & Therapeutics, 58,93-132 (1993)).
5) Yet another challenege for the crystallization of human interferon-alpha.13EA10 : The attempt failed as before indicating that there must be some fundamental reason for non-crystallizability. More systematic approaches making use of a dynamic light scattering device (for example) would be necessary.
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