Abstract
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 P2(1)2(1)2(1), with unit-cell parameters a = 47.8, b = 79.1, c = 141.8 Å. A Matthews coefficient V(M) of 2.6 Å(3) 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.