title: Purification, crystallization and preliminary X-ray diffraction analysis of aspartate semialdehyde dehydrogenase (Rv3708c) from Mycobacterium tuberculosis.
abstract: Aspartate semialdehyde dehydrogenase from Mycobacterium tuberculosis (Asd, ASADH, Rv3708c), which is the second enzyme in the lysine/homoserine-biosynthetic pathways, has been expressed heterologously in Escherichia coli. The enzyme was purified using affinity and gel-filtration chromatographic techniques and crystallized in two different crystal forms. Preliminary diffraction data analysis suggested the presence of up to four monomers in the asymmetric unit of the orthorhombic crystal form A and of one or two monomers in the cubic crystal form B.
authors.affiliation: Department of Biotechnology, Panjab University, Chandigarh 160 014, India.
authors.forename: Rajan
authors.initials: R
authors.lastname: Vyas
authors.forename: Vijay
authors.initials: V
authors.lastname: Kumar
authors.forename: Santosh
authors.initials: S
authors.lastname: Panjikar
authors.forename: Subramanian
authors.initials: S
authors.lastname: Karthikeyan
authors.forename: K V Radha
authors.initials: KV
authors.lastname: Kishan
authors.forename: Rupinder
authors.initials: R
authors.lastname: Tewari
authors.forename: Manfred S
authors.initials: MS
authors.lastname: Weiss
mesh_terms: D001223:Aspartate-Semialdehyde Dehydrogenase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D003460:Crystallization; D009169:Mycobacterium tuberculosis / Q000201:enzymology*; D014961:X-Ray Diffraction
chemical_list: D001223:Aspartate-Semialdehyde Dehydrogenase