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Crystallization and preliminary X-ray analysis of the Entamoeba histolytica α-actinin-2 rod domain
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen. (Lars Backman)
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
2011 (engelsk)Inngår i: Acta Crystallographica. Section F: Structural Biology and Crystallization Communications, ISSN 1744-3091, E-ISSN 1744-3091, Vol. 67, nr 10, s. 1214-1217Artikkel i tidsskrift (Fagfellevurdert) 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.

 

sted, utgiver, år, opplag, sider
International Union of Crystallography , 2011. Vol. 67, nr 10, s. 1214-1217
Emneord [en]
actinin, Entamoeba histolytica, actin-binding proteins
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Identifikatorer
URN: urn:nbn:se:umu:diva-44073DOI: 10.1107/S1744309111026066OAI: oai:DiVA.org:umu-44073DiVA, id: diva2:417900
Tilgjengelig fra: 2011-05-18 Laget: 2011-05-18 Sist oppdatert: 2018-06-08bibliografisk kontrollert

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