Crystallization and preliminary X-ray crystallographic analysis of Plasmodium falciparum S-adenosyl-L-homocysteine hydrolase

Protein Pept Lett. 2004 Apr;11(2):201-5. doi: 10.2174/0929866043478248.

Abstract

S-adenosyl-l-homocysteine hydrolase from a malaria parasite Plasmodium falciparum (PfSAHH) has been crystallized by the vapor diffusion method. The crystals belong to an orthorhombic space group P212121 with the cell dimensions of a = 76.66 A, b = 86.31 A, and c = 335.6 A. There are four subunits (one tetramer) per asymmetric unit. X-ray diffraction data have been collected up to 2.8 A resolution. Self-rotation function studies suggest that the tetrameric PfSAHH molecule has the 222 point group symmetry.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosylhomocysteinase / chemistry*
  • Animals
  • Crystallization
  • Crystallography, X-Ray
  • Plasmodium falciparum / enzymology*
  • Protozoan Proteins / chemistry*

Substances

  • Protozoan Proteins
  • Adenosylhomocysteinase