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タイトル
  • en High mobility of lattice molecules and defects during the early stage of protein crystallization
作成者
    • en Yamazaki, Tomoya
    • en Van Driessche, Alexander E. S.
アクセス権 open access
主題
  • NDC 440
内容注記
  • Abstract en Protein crystals are expected to be useful not only for their molecular structure analysis but also as functional materials due to their unique properties. Although the generation and the propagation of defects during crystallization play critical roles in the final properties of protein crystals, the dynamics of these processes are poorly understood. By time-resolved liquid-cell transmission electron microscopy, we observed that nanosized crystal defects are surprisingly mobile during the early stages of the crystallization of a lysozyme as a model protein. This highly dynamic behavior of defects reveals that the lattice molecules are mobile throughout the crystal structure. Moreover, the disappearance of the defects indicated that intermolecular bonds can break and reform rapidly with little energetic cost, as reported in theoretical studies. All these findings are in marked contrast to the generally accepted notion that crystal lattices are rigid with very limited mobility of individual lattice molecules.
出版者 en Royal Society of Chemistry
日付
    Issued2020-02-28
言語
  • eng
資源タイプ journal article
出版タイプ AM
資源識別子 HDL http://hdl.handle.net/2115/80511
関連
  • isVersionOf DOI https://doi.org/10.1039/c9sm02382h
収録誌情報
    • PISSN 1744-683X
      • en Soft matter
      • 16 8 開始ページ1955 終了ページ1960
ファイル
コンテンツ更新日時 2023-07-26