Skip to main content

Crystallization and Preliminary X-Ray Crystallographic Analysis of Plasmodium Falciparum S-Adenosyl-L-Homocysteine Hydrolase

Buy Article:

$55.00 plus tax (Refund Policy)

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 Å, b = 86.31 Å, and c = 335.6 Å. There are four subunits (one tetramer) per asymmetric unit. X-ray diffraction data have been collected up to 2.8 Å resolution. Selfrotation function studies suggest that the tetrameric PfSAHH molecule has the 222 point group symmetry.
No References
No Citations
No Supplementary Data
No Data/Media
No Metrics

Keywords: Plasmodium; S-adenosyl-L-homocysteine; hydrolase; orthorhombic

Document Type: Review Article

Affiliations: School of Pharmaceutical Sciences, Showa University, Tokyo 142-8555, JAPAN.

Publication date: 2004-04-01

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more