Image credit: Andrea Cellini, Weixiao Yuan Wahlgren, Léocadie Henry, Suraj Pandey, Swagatha Ghosh, Leticia Castillon, Elin Claesson, Heikki Takala, Joachim Kübel, Amke Nimmrich, Valentyna Kuznetsova, Eriko Nango, So Iwata, Shigeki Owada, Emina A. Stojkovic, Marius Schmidt, Janne A, Ihalainen and Sebastian Westenhoff. The three-dimensional structure of Drosophila melanogaster (6-4) photolyase at room temperature. Acta Crystallographica Section D, Volume 77, Part 8, August 2021, Pages 1001-1009. DOI: 10.1107/S2059798321005830 Figure 2 (a) & (b)

Cellini et al. reports the highest resolution structure at 1.79 Å found in the Protein Data Bank for Drosophila melanogaster (6-4) photolyase in the IUCr Journal, Acta Crystallographica Section D, Volume 77, Part 8, Pages 1001 - 1009, published August 2021. The macrocrystals were initially grown in a condition containing 0.2 M Lithium sulfate monohydrate, 0.1 M BIS-TRIS pH 6.5, 25% w/v Polyethylene glycol 3,350. Diffraction quality was optimized with the supplementation of 4% v/v Polypropylene glycol P 400, which was discovered from the use of the Additive Screen. The macrocystals were crushed with the Seed Bead kit to produce a crystal slurry that was used in a batch crystallization trial to grow the microcrystals needed for room temperature serial femtosecond crystallography.

The work performed has opened up future avenues for research on Dm(6-4)PL using serial femtosecond crystallography to further explore the structural workings of this light reactive protein.