Leishmania donovani coronin CRN12 is an actin‐binding protein which consists of two domains: an N‐terminal WD repeat domain and a C‐terminal coiled‐coil domain. The coiled‐coil domain is 53 residues in length. Helix–helix interactions in general and coiled coils in particular are ubiquitous in the structure of proteins and play a significant role in the association among proteins, including supramolecular assemblies and transmembrane receptors that mediate cellular signalling, transport and actin dynamics. The L. donovani coronin CRN12 coiled‐coil domain (5.8 kDa) was cloned, overexpressed, purified to homogeneity and the N‐terminal 6×His tag was successfully removed by thrombin cleavage. Crystals of recombinant L. donovani coronin CRN12 coiled‐coil domain were grown by vapour diffusion using a hanging‐drop setup. Diffraction‐quality crystals were obtained and data extending to 2.46 Å resolution were collected at 100 K on BM14, ESRF, Grenoble, France. The crystal belonged to the monoclinic space group C2, with unit‐cell parameters a = 118.0, b = 50.6, c = 46.0 Å, β = 111.0°. Matthews coefficient (VM) calculations suggested the presence of 4–6 molecules in the asymmetric unit, corresponding to a solvent content of ∼33–55%, and are consistent with self‐rotation function calculations.