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Figure 4
Optimization workflow for serial crystallography sample preparation. (a) Proposed workflow for microcrystal optimization, starting from purified protein through initial screening and detailed phase diagram analysis to identify crystallization boundaries. The optimal condition is then scaled up using batch or droplet methods into larger volumes suitable for SX experiments. (b) AtPdx1.3 crystals showed limited size changes when scaled from 10 µl to large volumes, indicating a volume-independent system at this scale. (c) Crystal size variation during scale-up of BpGmhA. Initial scale-up from 10 µl to 500 µl resulted in rod-shaped crystals up to ∼200 µm, requiring crystal size reduction by doubling the seed concentration for SX experiments. (d) Final optimized AtPdx1.3 and BpGmhA microcrystal suspensions suitable for SX experiments.

IUCrJ
Volume 13| Part 2| March 2026| Pages 159-168
ISSN: 2052-2525
https://doi.org/10.1107/S2052252526000448