Purification, crystallization and preliminary X-ray diffraction analysis of aspartate semialdehyde dehydrogenase (Rv3708c) from Mycobacterium tuberculosis.
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.
Vyas
Rajan
R
Department of Biotechnology, Panjab University, Chandigarh 160 014, India.
Kumar
Vijay
V
Panjikar
Santosh
S
Karthikeyan
Subramanian
S
Kishan
K V Radha
KV
Tewari
Rupinder
R
Weiss
Manfred S
MS
D001223:Aspartate-Semialdehyde Dehydrogenase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D003460:Crystallization; D009169:Mycobacterium tuberculosis / Q000201:enzymology*; D014961:X-Ray Diffraction
D001223:Aspartate-Semialdehyde Dehydrogenase