The macromolecular complex of ICP and falcipain-2 from Plasmodium: preparation, crystallization and preliminary X-ray diffraction analysis

Hansen, G.; Schwarzloh, B.; Rennenberg, A.; Heussler, Volker; Hilgenfeld, R. (2011). The macromolecular complex of ICP and falcipain-2 from Plasmodium: preparation, crystallization and preliminary X-ray diffraction analysis. Acta crystallographica. Section F - Structural biology and crystallization communications online, 67(Pt 11), pp. 1406-10. Oxford: Wiley-Blackwell 10.1107/S1744309111034592

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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 A. A complete diffraction data set was collected to a resolution of 2.6 A.

Item Type:

Journal Article (Original Article)

Division/Institute:

08 Faculty of Science > Department of Biology > Institute of Cell Biology
08 Faculty of Science > Department of Biology > Institute of Cell Biology > Malaria

UniBE Contributor:

Heussler, Volker

Subjects:

500 Science > 570 Life sciences; biology

ISSN:

1744-3091

Publisher:

Wiley-Blackwell

Language:

English

Submitter:

Factscience Import

Date Deposited:

04 Oct 2013 14:27

Last Modified:

12 Jul 2016 08:37

Publisher DOI:

10.1107/S1744309111034592

PubMed ID:

22102243

Web of Science ID:

000296793300021

URI:

https://boris.unibe.ch/id/eprint/10100 (FactScience: 215939)

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