Purification characterization and crystallization of Acanthamoeba profilin expressed in Escherichia coli

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

Research output: Contribution to journalArticle

26 Citations (Scopus)

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, β =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
StatePublished - 1994
Externally publishedYes

Fingerprint

Profilins
Acanthamoeba
Crystallization
Actins
Escherichia coli
Bacteriophage T7
Urea
Protein Isoforms
Fluorescence
Rabbits
tartaric acid

Keywords

  • Crystallization
  • Cytoskeleton
  • Expression
  • Profilin
  • Protein structure

ASJC Scopus subject areas

  • Virology

Cite this

Purification characterization and crystallization of Acanthamoeba profilin expressed in Escherichia coli. / Almo, Steven C.; Pollard, T. D.; Way, M.; Lattman, E. E.

In: Journal of Molecular Biology, Vol. 236, No. 3, 1994, p. 950-952.

Research output: Contribution to journalArticle

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