Purification characterization and crystallization of Acanthamoeba profilin expressed in Escherichia coli

S. C. Almo, T. D. Pollard, M. Way, E. E. Lattman

Research output: Contribution to journalArticle

26 Scopus citations

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 profilm from Acanthamoeba-based on fluorescence monitored urea denaturation, circular dichroisrn, actin-nuoleotide exchange rate and the Ka 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, α =109·6°. These crystals contain one molecule in the asymmetric unit and diffract to 2·0 Å.

Original languageEnglish (US)
Pages (from-to)950-952
Number of pages3
JournalJournal of Molecular Biology
Volume236
Issue number3
DOIs
StatePublished - Feb 24 1994
Externally publishedYes

Keywords

  • Crystallization
  • Cytoskeleton
  • Expression
  • Profilin
  • Protein structure

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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