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Updated: May 7, 2026

Aip1p Dynamics Are Altered by the R256H Mutation in Actin
Published on: July 30, 2014
Crystallization and preliminary structural characterization of the two actin isoforms of the malaria parasite
Saligram Prabhakar Bhargav1, Juha Vahokoski, Esa-Pekka Kumpula
1Department of Biochemistry, University of Oulu, PO Box 3000, 90014 Oulu, Finland.
Abstract:
Malaria is a devastating disease caused by apicomplexan parasites of the genus Plasmodium that use a divergent actin-powered molecular motor for motility and invasion. Plasmodium actin differs from canonical actins in sequence, structure and function. Here, the purification, crystallization and secondary-structure analysis of the two Plasmodium actin isoforms are presented. The recombinant parasite actins were folded and could be purified to homogeneity. Plasmodium actins I and II were crystallized in complex with the gelsolin G1 domain; the crystals diffracted to resolutions of 1.19 and 2.2 Å and belonged to space groups P2₁2₁2₁ and P2₁, respectively, each with one complex in the asymmetric unit.
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