Open AccessThe macromolecular complex of ICP and falcipain‐2 from Plasmodium : preparation, crystallization and preliminary X‐ray diffraction analysis
Author(s) -
Hansen Guido,
Schwarzloh Britta,
Rennenberg Annika,
Heussler Volker T.,
Hilgenfeld Rolf
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111034592
Subject(s) - proteases , cysteine protease , crystallization , plasmodium falciparum , cysteine , protease , recombinant dna , plasmodium berghei , resolution (logic) , chemistry , macromolecule , biochemistry , biology , enzyme , malaria , immunology , organic chemistry , artificial intelligence , gene , computer science
The malaria parasite Plasmodium depends on the tight control of cysteine‐protease activity throughout its life cycle. Recently, the characterization of a new class of potent inhibitors of cysteine proteases (ICPs) secreted by Plasmodium has been reported. Here, the recombinant production, purification and crystallization of the inhibitory C‐terminal domain of ICP from P. berghei in complex with the P. falciparum haemoglobinase falcipain‐2 is described. The 1:1 complex was crystallized in space group P 4 3 , with unit‐cell parameters a = b = 71.15, c = 120.09 Å. A complete diffraction data set was collected to a resolution of 2.6 Å.