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 K d for rabbit skeletal actin. This recombinant material crystallized from 80% saturated sodium potassium tartrate, yielding monoclinic crystals, space group C2, a =91·4 Å, b=37·4 Å, c =34·7 Å, β=109·6°. These crystals contain one molecule in the asymmetric unit and diffract to 2·0 Å.
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