Growth of giant two-dimensional crystal of protein molecules from a three-phase contact line

Yasuhiro Ikezoe, Yoshikazu Kumashiro, Kaoru Tamada, Takuro Matsui, Ichiro Yamashita, Kiyotaka Shiba, Masahiko Hara

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23 Citations (Scopus)

Abstract

A novel method to fabricate a two-dimensional (2D) crystal of protein molecules has been developed. The method enables us to control both the position of nucleation and the direction of the crystal growth. The crystal obtained using a protein molecule, ferritin, was found to be composed of a number of densely packed single crystal domains with an unprecedentedly large size of approximately 100 μm2. This method also reveals characteristic behavior of the spatiotemporal evolution of the crystal; for example, "fusion" of the crystal domains, which is never observed in an ordinary crystal composed of atoms or ions, was demonstrated. Our approach could have potential in fabricating extraordinarily large and highly ordered nanoparticle arrays of organic or inorganic materials.

Original languageEnglish
Pages (from-to)12836-12841
Number of pages6
JournalLangmuir
Volume24
Issue number22
DOIs
Publication statusPublished - Nov 18 2008
Externally publishedYes

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All Science Journal Classification (ASJC) codes

  • Materials Science(all)
  • Condensed Matter Physics
  • Surfaces and Interfaces
  • Spectroscopy
  • Electrochemistry

Cite this

Ikezoe, Y., Kumashiro, Y., Tamada, K., Matsui, T., Yamashita, I., Shiba, K., & Hara, M. (2008). Growth of giant two-dimensional crystal of protein molecules from a three-phase contact line. Langmuir, 24(22), 12836-12841. https://doi.org/10.1021/la802104f