| タイトル |
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Two types of amorphous protein particles facilitate crystal nucleation
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| 作成者 |
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Van Driessche, Alexander E. S.
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| アクセス権 |
open access |
| 主題 |
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nucleation
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protein
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lysozyme
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transmission electron microscopy
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in situ observation
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| 内容注記 |
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Abstract
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Nucleation, the primary step in crystallization, dictates the number of crystals, the distribution of their sizes, the polymorph selection, and other crucial properties of the crystal population. We used timeresolved liquid-cell transmission electron microscopy (TEM) to perform an in situ examination of the nucleation of lysozyme crystals. Our TEM images revealed that mesoscopic clusters, which are similar to those previously assumed to consist of a dense liquid and serve as nucleation precursors, are actually amorphous solid particles (ASPs) and act only as heterogeneous nucleation sites. Crystalline phases never form inside them. We demonstrate that a crystal appears within a noncrystalline particle assembling lysozyme on an ASP or a container wall, highlighting the role of heterogeneous nucleation. These findings represent a significant departure from the existing formulation of the two-step nucleation mechanism while reaffirming the role of noncrystalline particles. The insights gained may have significant implications in areas that rely on the production of protein crystals, such as structural biology, pharmacy, and biophysics, and for the fundamental understanding of crystallization mechanisms.
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| 出版者 |
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National Academy of Sciences.
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| 日付 |
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| 言語 |
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| 資源タイプ |
journal article |
| 出版タイプ |
AM |
| 資源識別子 |
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http://hdl.handle.net/2115/66517
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| 関連 |
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isVersionOf
DOI
https://doi.org/10.1073/pnas.1606948114
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| 収録誌情報 |
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Proceedings of the National Academy of Sciences of the United States of America (PNAS)
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巻114
号9
開始ページ2154
終了ページ2159
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| ファイル |
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| コンテンツ更新日時 |
2023-07-26 |
