Over the past decade, remarkable advancements in femtosecond X-ray free-electron lasers (XFELs) have brought about a profound transformation in structural biology. These XFELs have opened up exciting opportunities for conducting high-time resolution, room-temperature studies on protein structures and dynamics. This cutting-edge methodology involves exposing thousands of crystals to X-ray beams in random orientations at room temperature. These innovations have spurred the emergence of serial crystallography techniques, which have gained traction on more adaptable and readily accessible microfocus beamlines in synchrotron facilities. The primary focus of this thesis revolves around the development and implementation of serial synchrotron crystallography for proteins at the macromolecular beamlines BioMAX and MicroMAX, located at MAX IV Laboratory in Sweden. \newline This dissertation encompasses the development of two innovative sample delivery devices (Serial-X and AdaptoCell), incorporation of various fixed-target methods and preparation for TR-SSX. In Paper I, we introduced a novel approach for collecting data from oxygen-sensitive samples using fixed-target, complemented by the introduction of 3-D printed accessories. Paper III demonstrates the successful application of the methodology outlined in Paper I to determine the structure of CYP3A4. Paper II delves into the creation of the Serial-X flow cell, designed for efficient delivery of viscous samples, a tool that has now found utility on numerous beamlines worldwide. Lastly, in Paper IV, we present the first room-temperature serial synchrotron crystallography structure of spinach RuBisCo, along with the prepatory steps for a time-resolved SSX study of RuBisCO at BioMAX.