title: Crystallization and preliminary X-ray analysis of the Entamoeba histolytica α-actinin-2 rod domain.
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.
authors.affiliation: Department of Chemistry, Umeå University, SE-901 87 Umeå, Sweden. barbara.addario@chem.umu.se
authors.forename: Barbara
authors.initials: B
authors.lastname: Addario
authors.forename: Shenghua
authors.initials: S
authors.lastname: Huang
authors.forename: Uwe H
authors.initials: UH
authors.lastname: Sauer
authors.forename: Lars
authors.initials: L
authors.lastname: Backman
mesh_terms: D000185:Actinin / Q000032:analysis / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004748:Entamoeba histolytica / Q000737:chemistry*
chemical_list: D000185:Actinin
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