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. 2008 Mar 1;64(Pt 3):167-70.
doi: 10.1107/S1744309108002753. Epub 2008 Feb 23.

Purification, crystallization and preliminary X-ray diffraction analysis of aspartate semialdehyde dehydrogenase (Rv3708c) from Mycobacterium tuberculosis

Rajan Vyas  1 , Vijay Kumar, Santosh Panjikar, Subramanian Karthikeyan, K V Radha Kishan, Rupinder Tewari, Manfred S Weiss
Affiliations

Purification, crystallization and preliminary X-ray diffraction analysis of aspartate semialdehyde dehydrogenase (Rv3708c) from Mycobacterium tuberculosis

Rajan Vyas et al. Acta Crystallogr Sect F Struct Biol Cryst Commun. .

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.

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Figures

Figure 1
Figure 1
The two crystal forms of M. tuberculosis Asd. (a) Crystal form A; (b) crystal form B.
See this image and copyright information in PMC

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