Crystallization and preliminary crystallographic analysis of beta-hydroxyacyl ACP dehydratase (FabZ) from Plasmodium falciparum.
The malarial parasite Plasmodium falciparum synthesizes fatty acids by the type II mechanism. In this cycle, the dehydration of the beta-hydroxyacyl acyl carrier protein is catalyzed by FabZ. Purified FabZ has been crystallized using the hanging-drop vapour-diffusion and microbatch techniques. The crystals are orthorhombic, with space group I222 or I2(1)2(1)2(1) and unit-cell parameters a = 71.78, b = 81.99, c = 97.49 A. A complete data set to a resolution of 2.5 A has been collected under cryoconditions (100 K) using a MAR imaging-plate detector system mounted on a rotating-anode X-ray generator.
Lakshmi Swarna Mukhi
Pidugu
P
Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India.
Kumar Sharma
Shailendra
S
Kapoor
Mili
M
Surolia
Namita
N
Surolia
Avadhesha
A
Suguna
Kaza
K
D000213:Acyl Carrier Protein / Q000737:chemistry*; D000818:Animals; D002846:Chromatography, Affinity; D003460:Crystallization / Q000379:methods*; D018360:Crystallography, X-Ray / Q000379:methods*; D004746:Enoyl-CoA Hydratase / Q000737:chemistry*; D010963:Plasmodium falciparum / Q000201:enzymology*; D011994:Recombinant Proteins
D000213:Acyl Carrier Protein; D011994:Recombinant Proteins; D004746:Enoyl-CoA Hydratase