Abstract |
Tuberculosis remains the leading cause of mortality arising from a bacterial pathogen (Mycobacterium tuberculosis). There is an urgent need for the development of new antimycobacterial agents. The aromatic amino-acid pathway is essential for the survival of this pathogen and represents a target for structure-based drug design. Accordingly, the M. tuberculosis prephenate dehydratase has been cloned, expressed, purified and crystallized by the hanging-drop vapour-diffusion method using PEG 400 as a precipitant. The crystal belongs to the orthorhombic space group I222 or I2(1)2(1)2(1), with unit-cell parameters a = 98.26, b = 133.22, c = 225.01 angstroms, and contains four molecules in the asymmetric unit. A complete data set was collected to 3.2 angstroms resolution using a synchrotron-radiation source.
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Authors | Ana Luiza Vivan, Márcio Vinícius Bertacini Dias, Cristopher Z Schneider, Walter Filgueira de Azevedo Jr, Luiz Augusto Basso, Diógenes Santiago Santos |
Journal | Acta crystallographica. Section F, Structural biology and crystallization communications
(Acta Crystallogr Sect F Struct Biol Cryst Commun)
Vol. 62
Issue Pt 4
Pg. 357-60
(Apr 01 2006)
ISSN: 1744-3091 [Electronic] England |
PMID | 16582484
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- DNA Primers
- Recombinant Proteins
- Polyethylene Glycols
- Prephenate Dehydratase
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Topics |
- Crystallization
- DNA Primers
- Mycobacterium tuberculosis
(enzymology)
- Polyethylene Glycols
- Polymerase Chain Reaction
- Prephenate Dehydratase
(chemistry, genetics, isolation & purification, metabolism)
- Recombinant Proteins
(chemistry, metabolism)
- X-Ray Diffraction
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