Crystallization and preliminary crystallographic analysis of $\beta$-hydroxyacyl ACP dehydratase (FabZ) from Plasmodium falciparum

Mukhi, Pidugu Lakshmi Swarna and Sharma, Shailendra Kumar and Kapoor, Mili and Surolia, Namita and Surolia, Avadhesha and Suguna, Kaza (2004) Crystallization and preliminary crystallographic analysis of $\beta$-hydroxyacyl ACP dehydratase (FabZ) from Plasmodium falciparum. In: Acta Crystallographica Section D: Biological Crystallography, 60 (1). pp. 120-121.

PDF Crystallization-631.pdf Restricted to Registered users only Download (144Kb) | Request a copy

Abstract

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 $I2_12_12_1$ and unit-cell parameters a = 71.78, b = 81.99, c = 97.49 $\AA$ . A complete data set to a resolution of 2.5 $\AA$ has been collected under cryoconditions (100 K) using a MAR imaging-plate detector system mounted on a rotating-anode X-ray generator.

Item Type:	Journal Article
Additional Information:	The copyright belongs to International Union of Crystallography.
Department/Centre:	Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited:	23 Jan 2007
Last Modified:	19 Sep 2010 04:28
URI:	http://eprints.iisc.ernet.in/id/eprint/7307

Actions (login required)

View Item