In cellulo crystallography with a synchrotron for a human neuraminidase
| Project/Area Number |
16K18507
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Structural biochemistry
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| Research Institution | High Energy Accelerator Research Organization |
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Principal Investigator |
Koiwai Kotaro 大学共同利用機関法人高エネルギー加速器研究機構, 物質構造科学研究所, 研究員 (60620721)
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| Co-Investigator(Renkei-kenkyūsha) |
ITOH Kohji 徳島大学, 大学院医歯薬学研究部, 教授 (00184656)
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| Research Collaborator |
SENDA Toshiya
YUMOTO Fumiaki
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| Project Period (FY) |
2016-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2017: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2016: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
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| Keywords | リソソーム病 / ノイラミニダーゼ / 細胞内結晶 / 放射光 / 構造生物学 / 自由電子レーザー / ガラクトシアリドーシス / シアリドーシス / NEU1 / 再結晶化 / X線結晶構造解析 / ヒトノイラミニダーゼ |
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| Outline of Final Research Achievements |
The purpose of this research is to clarify a molecular mechanism why mutations causing lysosomal diseases on human neuraminidase-1 (NEU1) reduce its activity. During this period, methods to prepare NEU1 in cellulo crystals have been improved, and X-ray diffraction data were collected from the extracted crystals. Furthermore, high-quality protein solution has been prepared by using the improved method followed by purification. This work opens a way for not only on NEU1 structural analysis but for commonly in cellulo crystallography.
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Report
(3 results)
Research Products
(10 results)
