The three-dimensional structure of Drosophila melanogaster (6-4) photolyase at room temperature

Andrea Cellini, Weixiao Yuan Wahlgren, Leocadie Henry, Suraj Pandey, Swagatha Ghosh, Leticia Castillon, Elin Claesson, Heikki Takala, Joachim Kübel, Amke Nimmrich, Valentyna Kuznetsova, Eriko Nango, So Iwata, Shigeki Owad, Emina A. Stojkovic, Marius Schmid, Janne A. Ihalainen, Sebastian Westenhoff

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


(6-4) photolyases are flavoproteins that belong to the photolyase/cryptochrome family. Their function is to repair DNA lesions using visible light. Here, crystal structures of Drosophila melanogaster (6-4) photolyase [Dm(6-4)photolyase] at room and cryogenic temperatures are reported. The room-temperature structure was solved to 2.27 Å resolution and was obtained by serial femtosecond crystallography (SFX) using an X-ray free-electron laser. The crystallization and preparation conditions are also reported. The cryogenic structure was solved to 1.79 Å resolution using conventional X-ray crystallography. The structures agree with each other, indicating that the structural information obtained from crystallography at cryogenic temperature also applies at room temperature. Furthermore, UV-Vis absorption spectroscopy confirms that Dm(6-4)photolyase is photoactive in the crystals, giving a green light to time-resolved SFX studies on the protein, which can reveal the structural mechanism of the photoactivated protein in DNA repair.

Original languageEnglish
Pages (from-to)1001-1009
Number of pages9
JournalActa Crystallographica Section D: Structural Biology
Publication statusPublished - 2021 Aug 1


  • (6-4) photolyase
  • Drosophila melanogaster
  • FAD
  • Flavoproteins
  • Photolyases
  • Room-temperature structure
  • Serial crystallography

ASJC Scopus subject areas

  • Structural Biology


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