Crystallization technique of high-quality protein crystals controlling surface free energy

Haruhiko Koizumi, Satoshi Uda, Katsuo Tsukamoto, Masaru Tachibana, Kenichi Kojima, Junpei Okada, Jun Nozawa

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

The relationship between protein crystal quality and growth kinetics was assessed by measuring the normal growth rates vs supersaturation of the (110) and (101) faces of dislocation-free tetragonal hen egg white lysozyme crystals at three precipitant concentrations, with NaCl as the precipitant. Assuming a two-dimensional birth and spreading nucleation mechanism, an increase in the surface free energy of the step edges was realized with increasing NaCl concentration, as established by decreases in the full width at halfmaximum values of X-ray diffraction rocking curves obtained from crystals. These results demonstrate that controlling the surface free energy of the step edges is an important aspect of obtaining high-quality protein crystals. This work also proposes a mechanism for the observed improvements in the crystal quality, based on the reduced incorporation of impurities into the steps during crystal growth.

Original languageEnglish
Pages (from-to)6712-6718
Number of pages7
JournalCrystal Growth and Design
Volume17
Issue number12
DOIs
Publication statusPublished - 2017 Jan 1

ASJC Scopus subject areas

  • Chemistry(all)
  • Materials Science(all)
  • Condensed Matter Physics

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