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Two types of amorphous protein particles facilitate crystal nucleation
| Title: | Two types of amorphous protein particles facilitate crystal nucleation |
| Authors: | Yamazaki, Tomoya Browse this author | | Kimura, Yuki Browse this author →KAKEN DB | | Vekilov, Peter G. Browse this author | | Furukawa, Erika Browse this author | | Shirai, Manabu Browse this author | | Matsumoto, Hiroaki Browse this author | | Van Driessche, Alexander E. S. Browse this author | | Tsukamoto, Katsuo Browse this author |
| Keywords: | nucleation | | protein | | lysozyme | | transmission electron microscopy | | in situ observation |
| Issue Date: | 10-Jan-2017 |
| Publisher: | National Academy of Sciences. |
| Journal Title: | Proceedings of the National Academy of Sciences of the United States of America (PNAS) |
| Volume: | 114 |
| Issue: | 9 |
| Start Page: | 2154 |
| End Page: | 2159 |
| Publisher DOI: | 10.1073/pnas.1606948114 |
| Abstract: | 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. |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/66517 |
| Appears in Collections: | 低温科学研究所 (Institute of Low Temperature Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 木村 勇気
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