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Crystallization and preliminary X-ray crystallographic studies of the N-terminal domain of FadD28, a fatty-acyl AMP ligase from Mycobacterium tuberculosis
A. Goyal, M. Yousuf, , P. Arora, R.S. Gokhale, R. Sankaranarayanan
Published in
2006
PMID: 16582482
Volume: 62
   
Issue: 4
Pages: 350 - 352
Abstract
FadD28 from Mycobacterium tuberculosis belongs to the fatty-acyl AMP ligase (FAAL) family of proteins. It is essential for the biosynthesis of a virulent phthiocerol dimycocerosate (PDIM) lipid that is only found in the cell wall of pathogenic mycobacteria. The N-terminal domain, comprising of the first 460 residues, was crystallized by the hanging-drop vapour-diffusion method at 295 K. The crystals belong to space group P212121, with unit-cell parameters a = 50.97, b = 60.74, c = 136.54 Å. The crystal structure of the N-terminal domain of FadD28 at 2.35 Å resolution has been solved using the MAD method. © 2006 International Union of Crystallography. All rights reserved.
About the journal
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
ISSN17443091