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Purification, crystallization and preliminary X-ray diffraction analysis of aspartate semialdehyde dehydrogenase (Rv3708c) from Mycobacterium tuberculosisPublished in
2008
Volume: 64
Issue: 3
Pages: 167 - 170
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. {\textcopyright} International Union of Crystallography All rights reserved.
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Content may be subject to copyright,Check LicenseThe final published version can be found at https://doi.org/10.1107/S1744309108002753The final published version can be found at https://doi.org/10.1107/S1744309108002753
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Rajan Vyas- Biochemical and biophysical characterization of recombinant aspartate semialdehyde dehydrogenase ASD of mycobacterium tuberculosis H37Rv
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