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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.
- Source :
- Acta Crystallographica: Section F (Wiley-Blackwell); Apr2006, Vol. 62 Issue 4, p350-352, 3p, 1 Color Photograph, 1 Black and White Photograph, 1 Chart
- Publication Year :
- 2006
-
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 P2<subscript>1</subscript>2<subscript>1</subscript>2<subscript>1</subscript>, 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. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 17443091
- Volume :
- 62
- Issue :
- 4
- Database :
- Complementary Index
- Journal :
- Acta Crystallographica: Section F (Wiley-Blackwell)
- Publication Type :
- Academic Journal
- Accession number :
- 20386449
- Full Text :
- https://doi.org/10.1107/S1744309106005938