Due to advances at synchrotrons worldwide, fragment screening by X-ray crystallography has emerged as a robust way to screen the binding of large fragment libraries to a protein target. Using this structural information, fragments can then be elaborated with medicinal chemistry to generate drug-like lead compounds. The Australian Synchrotron (AS) is developing a fragment screening platform for aiding fragment-based drug discovery (FBDD). A key feature of this platform will be the unattended data collection which will be capable of automatically centering crystal samples based on an optical machine learning algorithm developed in-house. During testing, we were able to collect unattended datasets at a rate of up to 40 crystals per hour with a 93% success rate. The details of the fragment libraries being assembled by the AS for future users of the platform are also shared. Another key feature of the platform will be the integration of a crystal shifter X-Y stage instrument (Oxford Lab Technologies) that automates and speeds up crystal harvesting and freezing by four-fold. The overall design and adoption of the fragment screening platform onto the existing macromolecular X-ray crystallography (MX) beamlines, MX1 and MX2, are presented. Furthermore, the results from the first fragment screening campaign with SARS-Cov2 main protease (MPro) are shown. This platform will allow users to perform high-throughput X-ray crystallography and represents an important addition to the drug discovery toolkit within Australia.