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- W3191611541 abstract "(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." @default.
- W3191611541 created "2021-08-16" @default.
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- W3191611541 date "2021-07-29" @default.
- W3191611541 modified "2023-10-17" @default.
- W3191611541 title "The three-dimensional structure of <i>Drosophila melanogaster</i> (6–4) photolyase at room temperature" @default.
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- W3191611541 doi "https://doi.org/10.1107/s2059798321005830" @default.
- W3191611541 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8329860" @default.