ArticleActa crystallographica. Section F, Structural biology and crystallization communications2008
Purification, crystallization and preliminary crystallographic study of the putative enolase MJ0232 from the hyperthermophilic archaeon Methanococcus jannaschii.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2008. 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.
- Glucose Metabolism and Acetate Switch in Archaea: the Enzymes in Haloferax volcanii.Journal of bacteriology · 2021Article
- Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.Microbiology and molecular biology reviews : MMBR · 2014Review
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Abstract
Enolase is a glycolytic enzyme that catalyzes the interconversion of phosphoenolpyruvate and 2-phosphoglycerate. In order to gain insight into the biological significance of the oligomeric state of this enzyme, the putative enolase MJ0232 from the hyperthermophilic archaeon Methanococcus jannaschii was cloned, overexpressed and purified. Crystals were obtained by the oil-microbatch method at 291 K using PEG 4000 as a precipitant. A native data set was collected to 1.85 A resolution. The crystal belonged to the tetragonal space group I4, with unit-cell parameters a = 148.8, c = 91.2 A. An initial model was obtained by molecular replacement, which revealed an octameric subunit association (a tetramer of dimers). This result is consistent with that from a dynamic light-scattering experiment, suggesting biological relevance of the octameric state of MJ0232 in solution.
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