X-ray free-electron laser (XFEL) serial femtosecond crystallography (SFX) has enabled high-resolution structure determination from tiny microcrystals at room temperature, while outrunning structure-altering radiation damage. This has facilitated room temperature structure determination of hard-to-crystallise, radiation-sensitive targets, G protein-coupled receptors, and in vivo grown nano/microcrystals. The use of tiny microcrystals at room temperature permits rapid reaction initiation and allows the macromolecule to retain functionally relevant conformational flexibility, which may be disrupted by cryopreservation. The development of time-resolved SFX has made use of this for structural investigations of reaction dynamics with unprecedented temporal resolution in numerous systems and with multiple reaction initiation mechanisms. Meanwhile, microfocus beamlines at modern synchrotrons, coupled with fast frame-rate detectors and automated microcrystal sample delivery systems, are pushing the capabilities of synchrotron macromolecular crystallography to ever-smaller crystals and faster data collection. Serial snapshot crystallography at synchrotrons makes use of the data analysis and sample delivery tools invented for SFX to spread the radiation damage over many crystals, narrowing the gap between XFEL and synchrotron capabilities for room temperature microcrystallography. We will present results from the state-of-the-art in time-resolved SFX at XFELs, highlighting how it can help understand viral infection and antibiotic resistance. Then we will focus on recent advancements in serial snapshot micro-crystallography at synchrotrons, and the prospects for room-temperature time-resolved studies at the upcoming high-performance macromolecular crystallography (MX3) beamline at the Australian Synchrotron.