ArticleActa crystallographica. Section F, Structural biology communications2017
Crystallization and biochemical characterization of an archaeal lectin from Methanococcus voltae A3.
Article in Acta crystallographica. Section F, Structural biology communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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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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Who cites it
2 citing papers in PubMed.
- Structure of the hypothetical protein TTHA1873 from Thermus thermophilus.Acta crystallographica. Section F, Structural biology communications · 2022Article
- 'Clickable lectins': bioorthogonal reactive handles facilitate the directed conjugation of lectins in a modular fashion.Interface focus · 2019Article
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Authors and funding
3 authors.
Funding
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Abstract
A lectin from Methanococcus voltae A3 has been cloned, expressed, purified and characterized. The lectin appears to be specific for complex sugars. The protein crystallized in a tetragonal space group, with around 16 subunits in the asymmetric unit. Sequence comparisons indicate the lectin to have a β-prism I fold, with poor homology to lectins of known three-dimensional structure.
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Registered trials
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