Angiopoietin-related protein 4 (Angptl4) belongs to a family of eight proteins (Angptls) structurally similar to angiopoietins. They all possess an N-terminal coiled-coil domain, a disordered linker and a C-terminal fibrinogen-like domain. Angptl4 is involved in a variety of cellular processes, including angiogenesis and energy metabolism. Angptl4 plays a role in the lipid metabolism by inhibiting lipoprotein lipase. Recently, a C-terminal fibrinogen-like domain of Angptl4 was shown to interact and activate integrins β1 and β5 and their cognate extracellular matrix proteins to facilitate wound healing and enhance re-epithelialization. To clarify the role of Angptl4 in lipid metabolism and wound healing and identify protein determinants involved in interactions we determined the crystal structure of a fibrinogen-like domain of Angptl4 from human. The protein was produced using a system for the efficient production of disulfide bond containing proteins in the cytoplasm of E. coli, known as CyDisCo. A single crystal appeared in a crystallization screen and yielded in a 2.6 Å X-ray diffraction dataset. The crystal structure was solved by molecular replacement. Electrostatic surface potential analysis revealed the presence of an extensive positively charged patch on the exposed surface of one of the subdomains which is likely involved in binding of a ligand or interaction partner.