Overexpression, purification, crystallization and preliminary X-ray analysis of uracil N-glycosylase from Mycobacterium tuberculosis in complex with a proteinaceous inhibitor

Journal Article · Fri Dec 01 00:00:00 EST 2006 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309106045805· OSTI ID:22356407

Singh, Prem ^[1]; Talawar, Ramappa K.; Krishna, P. D. V.; Varshney, Umesh ^[2]

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1. Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012 (India)
2. Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore 560 012 (India)

Uracil N-glycosylase from M. tuberculosis has been crystallized in complex with a proteinaceous inhibitor (Ugi) and X-ray diffraction data have been collected. Uracil N-glycosylase is an enzyme which initiates the pathway of uracil-excision repair of DNA. The enzyme from Mycobacterium tuberculosis was co-expressed with a proteinaceous inhibitor from Bacillus subtilis phage and was crystallized in monoclinic space group C2, with unit-cell parameters a = 201.14, b = 64.27, c = 203.68 Å, β = 109.7°. X-ray data from the crystal have been collected for structure analysis.

• OSTI ID: 22356407
• Journal Information: Acta Crystallographica. Section F, Vol. 62, Issue Pt 12; Other Information: PMCID: PMC2225355; PMID: 17142904; PUBLISHER-ID: bw5179; OAI: oai:pubmedcentral.nih.gov:2225355; Copyright (c) International Union of Crystallography 2006; 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
CRYSTALLIZATION
CRYSTALS
DNA
SPACE GROUPS
X-RAY DIFFRACTION