Investigation of the mechanism of photochemically-induced lysozyme crystallization

Tetsuo Okutsu*, Tohru Taguchi, Jyunya Korenaga, Takashi Kuroiwa, Yu Ishikawa, Shiori Iizuka, Kaori Sugiyama, Hiroaki Horiuchi, Hiroshi Hiratsuka

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)


This work examined the mechanism involved in photoinduced crystallization of a lysozyme, focusing on the structure of the photoproducts that lead to crystal growth. It was determined that dimers formed via linking of tryptophan (Trp) residues are preferentially produced when applying a high-excitation photon fluence. However, these dimers do not lead to crystal growth. A low fluence forms dimers via the combination of tyrosine (Tyr) residues, generating six types of Tyr-Tyr dimers. The dimer that originates from the linking of Tyr53 and Tyr53 has a configuration similar to that of the two adjacent, yet non-linked, lysozyme molecules in the crystal unit cell. The Tyr53-Tyr53 dimer hence acts as a template for lysozyme crystal nucleation.

Original languageEnglish
Pages (from-to)180-186
Number of pages7
JournalJournal of Photochemistry and Photobiology A: Chemistry
Publication statusPublished - 2016 May 1
Externally publishedYes


  • Lysozyme
  • Photo-induced crystallization
  • Template

ASJC Scopus subject areas

  • Chemistry(all)
  • Chemical Engineering(all)
  • Physics and Astronomy(all)


Dive into the research topics of 'Investigation of the mechanism of photochemically-induced lysozyme crystallization'. Together they form a unique fingerprint.

Cite this