Crystallization and preliminary X-ray diffraction analysis of prephenate dehydratase from Mycobacterium tuberculosis H37Rv.
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.
Vivan
Ana Luiza
AL
Programa de Pós Graduação em Genética e Biologia Molecular, Departamento de Genética, Universidade Federal do Rio Grande do Sul, Porto Alegre, RS, Brazil.
Dias
Márcio Vinícius Bertacini
MV
Schneider
Cristopher Z
CZ
de Azevedo
Walter Filgueira
WF
Basso
Luiz Augusto
LA
Santos
Diógenes Santiago
DS
D003460:Crystallization; D017931:DNA Primers; D009169:Mycobacterium tuberculosis / Q000201:enzymology*; D011092:Polyethylene Glycols; D016133:Polymerase Chain Reaction; D011302:Prephenate Dehydratase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D014961:X-Ray Diffraction
D017931:DNA Primers; D011994:Recombinant Proteins; D011092:Polyethylene Glycols; D011302:Prephenate Dehydratase