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Crystallization and preliminary X-ray analysis of the Entamoeba histolytica α-actinin-2 rod domain
Umeå University, Faculty of Science and Technology, Department of Chemistry. (Lars Backman)
Umeå University, Faculty of Science and Technology, Department of Chemistry.
Umeå University, Faculty of Science and Technology, Department of Chemistry.
Umeå University, Faculty of Science and Technology, Department of Chemistry.
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
Abstract [en]

-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.
Keyword [en]
actinin, Entamoeba histolytica, actin-binding proteins
National Category
Chemical Sciences
Identifiers
URN: urn:nbn:se:umu:diva-44073DOI: 10.1107/S1744309111026066OAI: oai:DiVA.org:umu-44073DiVA: diva2:417900
Available from: 2011-05-18 Created: 2011-05-18 Last updated: 2017-12-11Bibliographically approved

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