ArticleActa crystallographica. Section F, Structural biology and crystallization communications2005
Expression, purification and crystallization of the ammonium transporter Amt-1 from Archaeoglobus fulgidus.
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 6 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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Who cites it
6 citing papers in PubMed, 17 citations in OpenAlex.
- Characterization ofBiotechnology for biofuels · 2018Article
- Review
- Characterization of three ammonium transporters of the glomeromycotan fungus Geosiphon pyriformis.Eukaryotic cell · 2013Article
- Detergent binding explains anomalous SDS-PAGE migration of membrane proteins.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Nitrogen metabolism in haloarchaea.Saline systems · 2008Article
- Crystal structure of the archaeal ammonium transporter Amt-1 from Archaeoglobus fulgidus.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ammonium transporters (Amts) are a class of membrane-integral transport proteins found in organisms from all kingdoms of life. Their key function is the transport of nitrogen in its reduced bioavailable form, ammonia, across cellular membranes, a crucial step in nitrogen assimilation for biosynthetic purposes. The genome of the hyperthermophilic archaeon Archaeoglobus fulgidus has been annotated with three individual genes for ammonium transporters, amt1-3, the roles of which are as yet unknown. The amt1 gene product has been produced by heterologous overexpression in Escherichia coli and the resulting protein has been purified to electrophoretic homogeneity. Crystals of Amt-1 have been obtained by sitting-drop vapour diffusion and diffraction data have been collected.
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