Purification, crystallization and preliminary X-ray diffraction analysis of aspartate semialdehyde dehydrogenase (Rv3708c) from Mycobacterium tuberculosis
Acta Crystallographica Section F
Volume 64, Issue 3, pages 167–170, March 2008
How to Cite
Vyas, R., Kumar, V., Panjikar, S., Karthikeyan, S., Kishan, K. V. R., Tewari, R. and Weiss, M. S. (2008), Purification, crystallization and preliminary X-ray diffraction analysis of aspartate semialdehyde dehydrogenase (Rv3708c) from Mycobacterium tuberculosis. Acta Crystallographica Section F, 64: 167–170. doi: 10.1107/S1744309108002753
- aspartate semialdehyde dehydrogenase;
- 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.