Crystallization of diphtheria toxin

J Mol Biol. 1991 Dec 20;222(4):861-4. doi: 10.1016/0022-2836(91)90577-s.


Two new crystal forms (forms III and IV) have been grown of diphtheria toxin (DT), which kills susceptible cells by catalyzing the ADP-ribosylation of elongation factor 2, thereby stopping protein synthesis. Forms III and IV diffract to 2.3 A and 2.7 A resolution, respectively. Both forms belong to space group C2; the unit cell parameters for form III are a = 107.3 A, b = 91.7 A, c = 66.3 A and beta = 94.7 degrees and those for form IV are a = 108.3 A, b = 92.3 A, c = 66.1 A and beta = 90.4 degrees. Both forms have one protein chain per asymmetric unit with the dimeric molecule on a twofold axis of symmetry. Form IV is exceptional among all crystal forms of DT in that it can be grown reproducibly. Thus the form IV crystals should yield a crystallographic structure giving insight into the catalytic, receptor-binding and membrane-insertion properties of DT.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Crystallization
  • Diphtheria Toxin / chemistry*
  • Diphtheria Toxin / isolation & purification
  • Indicators and Reagents
  • Protein Conformation
  • X-Ray Diffraction / methods


  • Diphtheria Toxin
  • Indicators and Reagents