ArticleActa crystallographica. Section F, Structural biology and crystallization communications2005
Cloning, expression, purification and preliminary crystallographic data for Rv3214 (EntD), a predicted cofactor-dependent phosphoglycerate mutase from Mycobacterium tuberculosis.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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2 citing papers in PubMed, 3 citations in OpenAlex.
- Two enzymes with redundant fructose bisphosphatase activity sustain gluconeogenesis and virulence in Mycobacterium tuberculosis.Nature communications · 2015Article
- Structural and functional analysis of Rv3214 from Mycobacterium tuberculosis, a protein with conflicting functional annotations, leads to its characterization as a phosphatase.Journal of bacteriology · 2006Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
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Abstract
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 A resolution and belong to space group P2(1), with unit-cell parameters a = 44.36, b = 79.03, c = 52.85 A, beta = 109.11 degrees. There are two molecules of molecular weight 21,948 Da per asymmetric unit.
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