Crystallographic characterization of tetanus toxin fragment C

J Mol Biol. 1993 Mar 20;230(2):673-4. doi: 10.1006/jmbi.1993.1181.

Abstract

The C-terminal fragment from tetanus toxin has been crystallized. The 50 kDa protein forms prismatic crystals with an orthorhombic unit cell of dimensions a = 64.03 A, b = 76.31 A and c = 135.3 A. The space group is P2(1)2(1)2(1). Assuming one molecule per asymmetric unit, the solvent occupies 63% of the unit cell.

MeSH terms

  • Crystallization
  • Indicators and Reagents
  • Molecular Weight
  • Peptide Fragments / chemistry*
  • Peptide Fragments / isolation & purification
  • Pichia / genetics
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Tetanus Toxin / chemistry*
  • Tetanus Toxin / isolation & purification
  • Toxins, Biological / chemistry
  • X-Ray Diffraction

Substances

  • Indicators and Reagents
  • Peptide Fragments
  • Recombinant Proteins
  • Tetanus Toxin
  • Toxins, Biological
  • tetanus toxin fragment C