Cloning, expression, purification and preliminary crystallographic data for Rv3214 (EntD), a predicted cofactor-dependent phosphoglycerate mutase from Mycobacterium tuberculosis
- Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720 (United States)
- Centre for Molecular Biodiscovery and School of Biological Sciences, University of Auckland, 3A Symonds Street, Private Bag 92019, Auckland (New Zealand)
A putative phosphoglycerate mutase from M. tuberculosis (Rv3214) has been crystallized. Diffraction data have been collected to 2.15 Å resolution from its selenomethionine-substituted form. The Mycobacterium tuberculosis open reading frame Rv3214, annotated as a cofactor-dependent phosphoglycerate mutase, has been cloned and expressed as an N-terminally His-tagged protein. Tagged, untagged and selenomethionine-labelled forms of Rv3214 (EntD) have been purified using nickel-affinity chromatography and gel filtration. The selenomethionine-labelled crystals diffracted to 2.15 Å resolution and belong to space group P2{sub 1}, with unit-cell parameters a = 44.36, b = 79.03, c = 52.85 Å, β = 109.11°. There are two molecules of molecular weight 21 948 Da per asymmetric unit.
- OSTI ID:
- 22356048
- Journal Information:
- Acta Crystallographica. Section F, Vol. 61, Issue Pt 8; Other Information: PMCID: PMC1952354; PMID: 16511148; PUBLISHER-ID: bw5096; OAI: oai:pubmedcentral.nih.gov:1952354; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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