Acne is one of the most common dermatological conditions, but the detailed pathology is unclear and current treatment regimens are plagued by side effects. Cutibacterium acnes is known as a major acne associated bacterium that derives energy from lipase mediated sebum lipid degradation. C. acnes is commensal, but free fatty acids digested by C. acnes lipases from triglyceride and lysophosphatidyl choline induce marked inflammation. Up to date, it remains to be elucidated the lipase activity mechanism at the molecular level. In this study, we report the purification and crystallization of the full-length lysophospholipase from C. acnes. The crystal diffracted X-rays to a 1.7 Å resolution, revealing that the crystals belong to space group P2₁2₁2, with cell dimension parameters of a = 94.5, b = 129.7, and c = 55.5 Å. Two protomers are present in the crystallographic asymmetric unit, with a calculated crystal volume per protein weight (V_M) of 2.50 ųDa^-1 and a solvent content of 50.79%. This structure will contribute towards revealing a detailed mechanism of acne development.