Crystallization of recombinant green mamba ρ-Da1a toxin during a lyophilization procedure and its structure determination

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jun;69(Pt 6):704-9. doi: 10.1107/S1744309113011470. Epub 2013 May 29.

Abstract

ρ-Da1a toxin from eastern green mamba (Dendroaspis angusticeps) venom is a polypeptide of 65 amino acids with a strong affinity for the G-protein-coupled α(1A)-adrenoceptor. This neurotoxin has been crystallized from resolubilized lyophilized powder, but the best crystals grew spontaneously during lyophilization. The crystals belonged to the trigonal space group P3(1)21, with unit-cell parameters a = b = 37.37, c = 66.05 Å, and diffracted to 1.95 Å resolution. The structure solved by molecular replacement showed strong similarities to green mamba muscarinic toxins.

Keywords: lyophilization; three-finger fold toxin; weak data.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Crystallization
  • Elapid Venoms / chemistry*
  • Elapid Venoms / genetics*
  • Elapidae*
  • Freeze Drying
  • Molecular Sequence Data
  • Peptides / chemistry*
  • Peptides / genetics*
  • Protein Folding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics

Substances

  • AdTx1 peptide, Dendroaspis angusticep
  • Elapid Venoms
  • Peptides
  • Recombinant Proteins

Associated data

  • PDB/4IYE