Purification, characterization and crystallization of human platelet profilin expressed in Escherichia coli

J Mol Biol. 1994 Aug 19;241(3):480-2. doi: 10.1006/jmbi.1994.1522.

Abstract

Human platelet profilin was expressed in Escherichia coli using a T7 based expression vector. The recombinant material is similar to authentic human platelet profilin based on the measured Kd for rabbit skeletal muscle actin. Crystals of the recombinant material were obtained from both PEG 8000 and (NH4)2SO4. These crystals are isomorphous and belong to the monoclinic space group C2, a = 75.0, b = 32.0, c = 62.5, beta = 123 degrees. These crystals contain one molecule in the asymmetric unit and diffract to at least 2.0 A.

MeSH terms

  • Actins / metabolism
  • Blood Platelets / chemistry
  • Contractile Proteins*
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli / genetics
  • Humans
  • Kinetics
  • Microfilament Proteins / chemistry*
  • Microfilament Proteins / genetics
  • Microfilament Proteins / isolation & purification
  • Microfilament Proteins / metabolism
  • Molecular Structure
  • Profilins
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism

Substances

  • Actins
  • Contractile Proteins
  • Microfilament Proteins
  • PFN1 protein, human
  • Profilins
  • Recombinant Proteins