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dc.contributor.authorSchilstra, M.
dc.contributor.authorSlot, J.W.
dc.contributor.authorVan der Meide, P.H.
dc.contributor.authorPosthuma, G.
dc.contributor.authorCremers, A.F.M.
dc.contributor.authorBosch, L.
dc.identifier.citationSchilstra , M , Slot , J W , Van der Meide , P H , Posthuma , G , Cremers , A F M & Bosch , L 1984 , ' Immunocytochemical localization of the elongation factor Tu in E. coli cells ' , FEBS Letters , vol. 165 , no. 2 , pp. 175-179 .
dc.identifier.otherPURE: 92019
dc.identifier.otherPURE UUID: 38c3a888-1697-421f-8040-5ab1016ffbf7
dc.identifier.otherdspace: 2299/3897
dc.identifier.otherScopus: 0021758417
dc.descriptionOriginal article can be found at: Copyright Federation of European Biochemical Societies. [Full text of this article is not available in the UHRA]
dc.description.abstractThe localization of the elongation factor Tu (EF-Tu) in ultrathin cryosections of E. coli cells was determined with the electron microscope using a highly specific immunological labellin technique. EF-Tu is distributed almost homogeneously throughout the cytoplasm. Although it has often been suggested that EF-Tu could be part of a putative prokaryotic cytoskeleton, we did not find any evidence for supramolecular assemblies, such as fibres or filaments, containing a large amount of EF-Tu. EF-Tu was not observed in association with the outer cell membrane and periplasmic space. A topological relationship with the inner membrane is not apparent in our micrographs. In cells in which the EF-Tu level is raised significantly, the protein piles up in discrete cell regions.en
dc.relation.ispartofFEBS Letters
dc.titleImmunocytochemical localization of the elongation factor Tu in E. coli cellsen
dc.contributor.institutionSchool of Computer Science
dc.description.statusPeer reviewed
rioxxterms.typeJournal Article/Review

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