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

Journal Article · Sat Mar 01 00:00:00 EST 2008 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309108002753· OSTI ID:22360485

Vyas, Rajan ^[1]; Kumar, Vijay ^[2]; Panjikar, Santosh ^[3]; Karthikeyan, Subramanian ^[2]; Kishan, K. V. Radha ^[2]; Tewari, Rupinder ^[1]

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1. Department of Biotechnology, Panjab University, Chandigarh 160 014 (India)
2. Institute of Microbial Technology, Sector 39-A, Chandigarh 160 036 (India)
3. EMBL Hamburg Outstation, c/o DESY, Notkestrasse 85, D-22603 Hamburg (Germany)

The enzyme aspartate semialdehyde dehydrogenase from M. tuberculosis has been expressed, purified and crystallized in two different crystal forms. 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.

• OSTI ID: 22360485
• Journal Information: Acta Crystallographica. Section F, Vol. 64, Issue Pt 3; Other Information: PMCID: PMC2374159; PMID: 18323599; PUBLISHER-ID: ll5139; OAI: oai:pubmedcentral.nih.gov:2374159; Copyright (c) International Union of Crystallography 2008; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
AFFINITY
CRYSTALLIZATION
CRYSTALS
DATA ANALYSIS
ESCHERICHIA COLI
GELS
LYSINE
MONOMERS
X-RAY DIFFRACTION