Crystallization and preliminary X-ray analysis of the Entamoeba histolytica α-actinin-2 rod domain

α-Actinins form antiparallel homodimers that are able to cross-link actin filaments. The protein contains three domains: an N-terminal actin-binding domain followed by a central rod domain and a calmodulin-like EF-hand domain at the C-terminus. Here, crystallization of the rod domain of Entamoeba histolytica α-actinin-2 is reported; it crystallized in space group P2₁2₁2₁, with unit-cell parameters a = 47.8, b = 79.1, c = 141.8 Å. A Matthews coefficient V_M of 2.6 ų Da⁻¹ suggests that there are two molecules and 52.5% solvent content in the asymmetric unit. A complete native data set extending to a d-spacing of 2.8 Å was collected on beamline I911-2 at MAX-lab, Sweden.