title: Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of DapA (Rv2753c) from Mycobacterium tuberculosis.
abstract: Dihydrodipicolinate synthase from Mycobacterium tuberculosis (DHDPS, DapA, Rv2753c) has been cloned, heterologously expressed in Escherichia coli, purified using standard chromatographic techniques and crystallized in a monoclinic crystal form. Preliminary diffraction data analysis suggests the presence of two independent tetramers in the asymmetric unit in almost the same relative orientation.
authors.affiliation: EMBL Hamburg Outstation, c/o DESY, Notkestrasse 85, D-22603 Hamburg, Germany.
authors.forename: Georgia
authors.initials: G
authors.lastname: Kefala
authors.forename: Manfred S
authors.initials: MS
authors.lastname: Weiss
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification; D001483:Base Sequence; D003001:Cloning, Molecular; D017931:DNA Primers; D006836:Hydro-Lyases / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D009169:Mycobacterium tuberculosis / Q000201:enzymology*; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D014961:X-Ray Diffraction
chemical_list: D001426:Bacterial Proteins; D017931:DNA Primers; D011994:Recombinant Proteins; D006836:Hydro-Lyases; C020040:4-hydroxy-tetrahydrodipicolinate synthase