In cellulo crystallography with a synchrotron for a human neuraminidase

2017 Fiscal Year Final Research Report

• Project/Area Number: 16K18507
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Structural biochemistry
• Research Institution: High Energy Accelerator Research Organization
• 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)
• Co-Investigator(Renkei-kenkyūsha): ITOH Kohji 徳島大学, 大学院医歯薬学研究部, 教授 (00184656)
• Research Collaborator: SENDA Toshiya ; YUMOTO Fumiaki
• Project Period (FY): 2016-04-01 – 2018-03-31
• 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

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.

Free Research Field

構造生物学