Human MAGL protein (1-303) with mutations Lys36Ala, Leu169Ser, and Leu176Ser (Cepter Biopartners, Nutley, NJ, USA) was concentrated to 10.8 mg/mL. crystalization trials were performed in sitting drop vapour diffusion setups at 21 °C. Crystals appeared within 2 days out of 0.1 M MES pH 6.5, 6-13% PEG MME5K, 12% isopropanol. Crystals were soaked for 16 h in a crystalization solution supplemented with 10 mM of the compounds. For data collection, crystals were flash-cooled at 100 K with 20% ethylene glycol added as a cryo-protectant to the soaking solution. Xray diffraction data were collected at a wavelength of 0.9999 Å using an Eiger2X 16M detector at the beamline X10SA of the Swiss Light Source (Villigen, Switzerland). Data have been processed with XDS and scaled with SADABS (Bruker, Billerica, MA, USA). The crystals belong to the space group C2221 with cell axes of a = 89.96 Å, b = 127.45 Å, c = 63.03 Å with and diffract to a resolution of 1.65 Å. The structure was determined by molecular replacement with PHASER using the coordinates of PDB entry 3PE6 as a search model . Difference electron density was used to place the compounds. The structure was refined with programs from the CCP4 suite and Buster. Model building was done with COOT . Data collection and refinement statistics are summarized in the SI (SI2.5).