title: Purification, crystallization and preliminary X-ray diffraction analysis of aspartate semialdehyde dehydrogenase (Rv3708c) from Mycobacterium tuberculosis.
creator: Vyas, Rajan
creator: Kumar, Vijay
creator: Panjikar, Santosh
creator: Karthikeyan, Subramanian
creator: Kishan, K V Radha
creator: Tewari, Rupinder
creator: Weiss, Manfred S
subject: QD Chemistry
description: 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.
publisher: International Union of Crystallography
date: 2008-03-01
type: Article
type: PeerReviewed
format: application/pdf
identifier: http://crdd.osdd.net/open/1077/1/karthikeyan2008.pdf
relation: http://scripts.iucr.org/cgi-bin/paper?S1744309108002753
identifier:   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     
relation: http://crdd.osdd.net/open/1077/