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  • Title: Purification, characterization and crystallization of Acanthamoeba profilin expressed in Escherichia coli.
    Author: Almo SC, Pollard TD, Way M, Lattman EE.
    Journal: J Mol Biol; 1994 Feb 25; 236(3):950-2. PubMed ID: 8114104.
    Abstract:
    Profilin (isoform I) from Acanthamoeba castellani was expressed in Escherichia coli using a bacteriophage T7-based expression vector. The recombinant material is similar to authentic profilin from Acanthamoeba-based on fluorescence monitored urea denaturation, circular dichroism, actin-nucleotide exchange rate and the Kd for rabbit skeletal actin. This recombinant material crystallized from 80% saturated sodium potassium tartrate, yielding monoclinic crystals, space group C2, a = 91.4 A, b = 37.4 A, c = 34.7 A, beta = 109.6 degrees. These crystals contain one molecule in the asymmetric unit and diffract to 2.0 A.
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