TY  - JOUR
ID  - open1077
UR  - http://scripts.iucr.org/cgi-bin/paper?S1744309108002753
IS  - Pt 3
A1  - Vyas, Rajan
A1  - Kumar, Vijay
A1  - Panjikar, Santosh
A1  - Karthikeyan, Subramanian
A1  - Kishan, K V Radha
A1  - Tewari, Rupinder
A1  - Weiss, Manfred S
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.
VL  - 64
TI  - Purification, crystallization and preliminary X-ray diffraction analysis of aspartate semialdehyde dehydrogenase (Rv3708c) from Mycobacterium tuberculosis.
AV  - restricted
EP  - 70
N1  - Copyright of this article belongs toInternational Union of Crystallography.
Y1  - 2008/03/01/
PB  - International Union of Crystallography
JF  - Acta crystallographica. Section F, Structural biology and crystallization communications
KW  - aspartate semialdehyde dehydrogenase; Mycobacterium tuberculosis; Rv3708c.
SN  - 1744-3091
SP  - 167
ER  -