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

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

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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.

Original languageEnglish
Pages (from-to)167-170
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number3
Publication statusPublished - 2008
Externally publishedYes


  • Aspartate semialdehyde dehydrogenase
  • Mycobacterium tuberculosis
  • Rv3708c

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