ArticleActa crystallographica. Section F, Structural biology and crystallization communications2010
Expression, purification, crystallization and preliminary X-ray analysis of the EIICGlc domain of the Escherichia coli glucose transporter.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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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3 citing papers in PubMed, 8 citations in OpenAlex.
- Structure and mechanism of a phosphotransferase system glucose transporter.Nature communications · 2024Article
- Structure, dynamics and biophysics of the cytoplasmic protein-protein complexes of the bacterial phosphoenolpyruvate: sugar phosphotransferase system.Trends in biochemical sciences · 2013Review
- Increasing the X-ray diffraction power of protein crystals by dehydration: the case of bovine serum albumin and a survey of literature data.International journal of molecular sciences · 2012Article
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5 authors at 2 institutions in 2 countries.
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Abstract
The glucose-import system of Escherichia coli consists of a hydrophilic EIIA(Glc) subunit and a transmembrane EIICB(Glc) subunit. EIICB(Glc) (UniProt P69786) contains two domains: the transmembrane EIIC(Glc) domain (40.6 kDa) and the cytoplasmic EIIB(Glc) domain (8.0 kDa), which are fused by a linker that is strongly conserved among its orthologues. The EIICB(Glc) subunit can be split within this motif by trypsin. Here, the crystallization of the tryptic EIIC(Glc) domain is described. A complete data set was collected to 4.5 A resolution at 100 K.
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