Fragment screening with X-ray crystallography was performed at Diamond Light Synchrotron (DLS) using the XChem pipeline developed at the I04-1 beamline. Purified PaFabF C164Q (15 mg/mL) and crystallization buffer (0.20 M ammonium format and 26% PEG 3350) were shipped to DLS on dry ice. The protein was crystallized at the DLS as described before. Briefly, 0.15 L of FabF C164Q protein solution was mixed with 0.15 L of crystallization buffer and let to equilibrate at 25 °C using the hanging drop vapor diffusion method over 60 L of crystallization buffer in a 96 well plate (3 drops per well).