title: Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the L,D-transpeptidase LdtMt1 from Mycobacterium tuberculosis.
abstract: Mycobacterium tuberculosis is capable of adapting to prolonged periods of dormancy, a state which is resistant to killing by antimycobacterial agents. The L,D-transpeptidation reaction catalysed by the L,D-transpeptidase LdtMt1 is likely to play an essential role in the adaptation of M. tuberculosis to its dormant state. LdtMt1 has been successfully crystallized using vapour-diffusion methods. The crystals of this protein belonged to space group P6₅22, with unit-cell parameters a=57.25, b=57.25, c=257.96 Å, α=90, β=90, γ=120°. Diffraction data have also been collected from a selenomethionine derivative to 2.9 Å resolution. Model building using the phases derived from the multiwavelength anomalous dispersion experiment is in progress.
authors.affiliation: Institute of Biostructures and Bioimaging, CNR, Via Mezzocannone 16, I-80134 Napoli, Italy.
authors.forename: Stefania
authors.initials: S
authors.lastname: Correale
authors.forename: Alessia
authors.initials: A
authors.lastname: Ruggiero
authors.forename: Emilia
authors.initials: E
authors.lastname: Pedone
authors.forename: Rita
authors.initials: R
authors.lastname: Berisio
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry / Q000235:genetics; D009169:Mycobacterium tuberculosis / Q000737:chemistry* / Q000201:enzymology; D010458:Peptidyl Transferases / Q000737:chemistry* / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D012645:Selenomethionine / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D011994:Recombinant Proteins; D012645:Selenomethionine; D010458:Peptidyl Transferases
keywords: LdtMt1; Mycobacterium tuberculosis; peptidoglycan; tuberculosis