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Two types of amorphous protein particles facilitate crystal nucleation

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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/66517

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)

Submitter: 木村 勇気

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