TY - JOUR
T1 - Purification, crystallization and preliminary X-ray diffraction analysis of aspartate semialdehyde dehydrogenase (Rv3708c) from Mycobacterium tuberculosis
AU - Vyas, Rajan
AU - Kumar, Vijay
AU - Panjikar, Santosh
AU - Karthikeyan, Subramanian
AU - Kishan, K. V.Radha
AU - Tewari, Rupinder
AU - Weiss, Manfred S.
PY - 2008
Y1 - 2008
N2 - 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.
AB - 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.
KW - Aspartate semialdehyde dehydrogenase
KW - Mycobacterium tuberculosis
KW - Rv3708c
UR - https://www.scopus.com/pages/publications/40449104686
U2 - 10.1107/S1744309108002753
DO - 10.1107/S1744309108002753
M3 - Article
C2 - 18323599
AN - SCOPUS:40449104686
SN - 1744-3091
VL - 64
SP - 167
EP - 170
JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications
JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications
IS - 3
ER -
