Crystallization and preliminary X-ray analysis of dihydrodipicolinate synthase from Clostridium botulinum in the presence of its substrate pyruvate

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Mar 1;65(Pt 3):253-5. doi: 10.1107/S1744309108039018. Epub 2009 Feb 14.


In this paper, the crystallization and preliminary X-ray diffraction analysis to near-atomic resolution of DHDPS from Clostridium botulinum crystallized in the presence of its substrate pyruvate are presented. The enzyme crystallized in a number of forms using a variety of PEG precipitants, with the best crystal diffracting to 1.2 A resolution and belonging to space group C2, in contrast to the unbound form, which had trigonal symmetry. The unit-cell parameters were a = 143.4, b = 54.8, c = 94.3 A, beta = 126.3 degrees . The crystal volume per protein weight (V(M)) was 2.3 A(3) Da(-1) (based on the presence of two monomers in the asymmetric unit), with an estimated solvent content of 46%. The high-resolution structure of the pyruvate-bound form of C. botulinum DHDPS will provide insight into the function and stability of this essential bacterial enzyme.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Clostridium botulinum / enzymology*
  • Crystallization
  • Crystallography, X-Ray
  • Hydro-Lyases / chemistry*
  • Pyruvic Acid / chemistry*
  • Recombinant Proteins / chemistry
  • Substrate Specificity


  • Recombinant Proteins
  • Pyruvic Acid
  • Hydro-Lyases
  • 4-hydroxy-tetrahydrodipicolinate synthase