title: The macromolecular complex of ICP and falcipain-2 from Plasmodium: preparation, crystallization and preliminary X-ray diffraction analysis.
abstract: 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 P4(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.
authors.affiliation: Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck, Germany.
authors.forename: Guido
authors.initials: G
authors.lastname: Hansen
authors.forename: Britta
authors.initials: B
authors.lastname: Schwarzloh
authors.forename: Annika
authors.initials: A
authors.lastname: Rennenberg
authors.forename: Volker T
authors.initials: VT
authors.lastname: Heussler
authors.forename: Rolf
authors.initials: R
authors.lastname: Hilgenfeld
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D003546:Cysteine Endopeptidases / Q000737:chemistry* / Q000378:metabolism; D015853:Cysteine Proteinase Inhibitors / Q000737:chemistry* / Q000378:metabolism; D010963:Plasmodium falciparum / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding
chemical_list: D015853:Cysteine Proteinase Inhibitors; D003546:Cysteine Endopeptidases; C416224:falcipain 2
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