Purification, crystallization and preliminary crystallographic studies on the N-terminal fragment of human protein disulfide isomerase

Acta Crystallogr D Biol Crystallogr. 1999 Nov;55(Pt 11):1958-60. doi: 10.1107/s0907444999011762.

Abstract

A fragment of human protein disulfide isomerase composed of the thioredoxin-like a and b domains (ab) has been expressed in Escherichia coli as a fusion protein with glutathione-S-transferase and purified after thrombin cleavage. Two forms of ab crystal were obtained with polyethylene glycol as precipitant and different additives at pH 7.5. The space group of form I is P4(1)2(1)2 or P4(3)2(1)2, with unit-cell dimensions a = 81.5, c = 259.7 A. The space group of form II is P4(1)22 or P4(3)22, with unit-cell dimensions a = 82.7, c = 86.5 A.

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Humans
  • Peptide Fragments / chemistry
  • Polyethylene Glycols
  • Protein Disulfide-Isomerases / chemistry*
  • Recombinant Proteins / chemistry
  • Thioredoxins / chemistry

Substances

  • Peptide Fragments
  • Recombinant Proteins
  • Polyethylene Glycols
  • Thioredoxins
  • Protein Disulfide-Isomerases