Importance of Determination of Crystal Quality in Protein Crystals when Performing High-Resolution Structural Analysis

Haruhiko Koizumi, Ryo Suzuki, Masaru Tachibana, Katsuo Tsukamoto, Izumi Yoshizaki, Seijiro Fukuyama, Yoshihisa Suzuki, Satoshi Uda, Kenichi Kojima

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)

Abstract

We show that the extinction effect explained by the dynamical theory of diffraction must be considered even in the case of protein crystals. Equal-thickness fringes, which are attributed to the Pendellösung effect, were clearly observed in the region of a tapered glucose isomerase crystal with wedge-like edges using X-ray topography carried out with a beam of monochromatic synchrotron radiation. This indicates that the perfection of this glucose isomerase crystal is high enough to produce this dynamical theory-related effect: this surely leads to difficulty in the collection of accurate integrated intensities of diffraction spots for X-ray structural analysis. Therefore, it is important to determine whether the crystal quality of a protein crystal under analysis is adequate to obtain accurate three-dimensional structures of protein molecules for X-ray structural analyses. We show that X-ray diffraction rocking-curve measurements can provide clues for this determination.

Original languageEnglish
Pages (from-to)4905-4909
Number of pages5
JournalCrystal Growth and Design
Volume16
Issue number9
DOIs
Publication statusPublished - 2016 Sep 7

ASJC Scopus subject areas

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

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