biostudies-literatureAkkaladevi NHHS | NIH | National Institute of General Medical SciencesNIGMS NIH HHSe00593-17https://www.ebi.ac.uk/biostudies/studies/S-EPMC5809691biostudies-literatureUnknown200(5)Transmembrane bacterial chemoreceptors are extended, rod-shaped homodimers with ligand-binding sites at one end and interaction sites for signaling complex formation and histidine kinase control at the other. There are atomic-resolution structures of chemoreceptor fragments but not of intact, membrane-inserted receptors. Electron tomography of <i>in vivo</i> signaling complex arrays lack distinct densities for chemoreceptor rods away from the well-ordered base plate region, implying structural heterogeneity. We used negative staining, transmission electron microscopy, and image analysis to characterize the molecular shapes of intact homodimers of the <i>Escherichia coli</i> aspartate receptor Tar rendered functional by insertion into nanodisc-provided <i>E. coli</i> lipid bilayers. Single-Journal of bacteriologyFlexible Hinges in Bacterial Chemoreceptors.PMC5809691GM29963R37 GM029963R01 GM029963Hazelbauer GLWhite TAStalla DBunyak FAkkaladevi NfalseFlexible Hinges in Bacterial Chemoreceptors.Transmembrane bacterial chemoreceptors are extended, rod-shaped homodimers with ligand-binding sites at one end and interaction sites for signaling complex formation and histidine kinase control at the other. There are atomic-resolution structures of chemoreceptor fragments but not of intact, membrane-inserted receptors. Electron tomography of <i>in vivo</i> signaling complex arrays lack distinct densities for chemoreceptor rods away from the well-ordered base plate region, implying structural heterogeneity. We used negative staining, transmission electron microscopy, and image analysis to characterize the molecular shapes of intact homodimers of the <i>Escherichia coli</i> aspartate receptor Tar rendered functional by insertion into nanodisc-provided <i>E. coli</i> lipid bilayers. Single-2018-01-01T00:00:00Z2018 Mar2026-05-06T03:45:21.471Z2019-03-26T23:49:44ZS-EPMC58096912922970010.1128/JB.00593-1710.1128/jb.00593-17