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

Vyas, Rajan and Kumar, Vijay and Panjikar, Santosh and Karthikeyan, Subramanian and Kishan, K V Radha and Tewari, Rupinder and Weiss, Manfred S (2008) Purification, crystallization and preliminary X-ray diffraction analysis of aspartate semialdehyde dehydrogenase (Rv3708c) from Mycobacterium tuberculosis. Acta crystallographica. Section F, Structural biology and crystallization communications, 64 (Pt 3). pp. 167-70. ISSN 1744-3091

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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.

Item Type:	Article
Additional Information:	Copyright of this article belongs toInternational Union of Crystallography.
Uncontrolled Keywords:	aspartate semialdehyde dehydrogenase; Mycobacterium tuberculosis; Rv3708c.
Subjects:	Q Science > QD Chemistry
Depositing User:	Dr. K.P.S.Sengar
Date Deposited:	21 Feb 2012 18:06
Last Modified:	21 Feb 2012 18:06
URI:	http://crdd.osdd.net/open/id/eprint/1077

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