Open AccessCrystallization and preliminary X‐ray diffraction analysis of prephenate dehydratase from Mycobacterium tuberculosis H37Rv
Author(s) -
Vivan Ana Luiza,
Dias Márcio Vinícius Bertacini,
Schneider Cristopher Z.,
De Azevedo Walter Filgueira,
Basso Luiz Augusto,
Santos Diógenes Santiago
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106006385
Subject(s) - mycobacterium tuberculosis , antimycobacterial , orthorhombic crystal system , dehydratase , tuberculosis , pathogen , crystallography , chemistry , stereochemistry , biology , microbiology and biotechnology , crystal structure , biochemistry , medicine , enzyme , pathology
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 I 222 or I 2 1 2 1 2 1 , with unit‐cell parameters a = 98.26, b = 133.22, c = 225.01 Å, and contains four molecules in the asymmetric unit. A complete data set was collected to 3.2 Å resolution using a synchrotron‐radiation source.