SX is especially valuable for studying proteins that do not readily form large, high-quality crystals, as well as for capturing ultrafast (femtosecond to millisecond) dynamic processes through time-resolved experiments. SX experiments entail the sequential illumination of numerous protein crystals using high-intensity X-ray beams, both at Free Electron Lasers (FEL) and synchrotrons. A fundamental challenge comes from the fact that SX generates massive datasets, often comprising thousands to millions of diffraction patterns, as it records a plethora of individual snapshots from numerous crystals to elucidate the threedimensional structures of molecules.