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Crystallization and preliminary X-ray diffraction analysis of prephenate dehydratase from Mycobacterium tuberculosis H37Rv.

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.
AuthorsAna Luiza Vivan, Márcio Vinícius Bertacini Dias, Cristopher Z Schneider, Walter Filgueira de Azevedo Jr, Luiz Augusto Basso, Diógenes Santiago Santos
JournalActa 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
PMID16582484 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • DNA Primers
  • Recombinant Proteins
  • Polyethylene Glycols
  • Prephenate Dehydratase
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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