Evaluation of protein crystal defects in real and reciprocal space by in situ observation

2020 Fiscal Year Final Research Report

• Project/Area Number: 18K14134
• Research Category: Grant-in-Aid for Early-Career Scientists
• Allocation Type: Multi-year Fund
• Review Section: Basic Section 30010:Crystal engineering-related
• Research Institution: Hokkaido University
• Principal Investigator: Yamazaki Tomoya 北海道大学, 低温科学研究所, 特別研究員(PD) (50735032)
• Project Period (FY): 2018-04-01 – 2021-03-31
• Keywords: タンパク質結晶 / 透過型電子顕微鏡 / 溶液セル / 結晶欠陥

Outline of Final Research Achievements

The dynamic behavior of defects in protein crystals, which degrade the quality of protein crystals, has been successfully visualized by transmission electron microscopy. The voids and the block structure were observed in protein crystals of micron size or smaller and their formation, movement, and disappearance were also observed. Analysis of these behaviors revealed that there is no time dependence on number density of defects in each crystal. This suggests that the defects originated before the crystals reached micron size, i.e., before, or immediately after nucleation.

Free Research Field

結晶成長

Academic Significance and Societal Importance of the Research Achievements

結晶の質を悪くする欠陥の動きの可視化に成功したことは、その欠陥が導入される原因を排除できることに繋がる。これは欠陥が導入される原理解明や高品質な結晶を育成するための指針となる。また、タンパク質の機能を理解したり、創薬に応用したりするためにはタンパク質分子の構造（形）を知る必要があり、これは調べたいタンパク質分子の高品質な結晶を作製して行う。より高品質な結晶を用いることで詳細なタンパク質分子の構造を知ることができる。