Crystallization and preliminary X-ray analysis of the Entamoeba histolytica α-actinin-2 rod domain
2011 (English)In: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications, ISSN 1744-3091, E-ISSN 1744-3091, Vol. 67, no 10, 1214-1217 p.Article in journal (Refereed) Published
-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 -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 VM of 2.6 Å3 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.
Place, publisher, year, edition, pages
International Union of Crystallography , 2011. Vol. 67, no 10, 1214-1217 p.
actinin, Entamoeba histolytica, actin-binding proteins
IdentifiersURN: urn:nbn:se:umu:diva-44073DOI: 10.1107/S1744309111026066OAI: oai:DiVA.org:umu-44073DiVA: diva2:417900