TY - JOUR
T1 - The macromolecular complex of ICP and falcipain-2 from Plasmodium: Preparation, crystallization and preliminary X-ray diffraction analysis
AU - Hansen, Guido
AU - Schwarzloh, Britta
AU - Rennenberg, Annika
AU - Heussler, Volker T.
AU - Hilgenfeld, Rolf
PY - 2011/11/1
Y1 - 2011/11/1
N2 - 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 P43, 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.
AB - 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 P43, 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.
UR - http://www.scopus.com/inward/record.url?scp=80955133162&partnerID=8YFLogxK
U2 - 10.1107/S1744309111034592
DO - 10.1107/S1744309111034592
M3 - Journal articles
C2 - 22102243
AN - SCOPUS:80955133162
VL - 67
SP - 1406
EP - 1410
JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications
JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications
SN - 1744-3091
IS - 11
ER -
