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tec 30s ic structure  (Thermo Fisher)


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    Structured Review

    Thermo Fisher tec 30s ic structure
    A Schematic of the ompD transcript and MicC recognition site. B , C Cleavage time courses of ompD mRNA fragment and +83-cleavage intermediate species (see Fig. and Suppl. Fig. for representative raw data). Free ompD mRNA fragment (black), ompD 89 -TEC (green), ompD 89 -30S IC (grey) and ompD 89 -TEC-IC (red) were incubated with MicC/Hfq and then subjected to cleavage by the RNA degradosome. Reactions were stopped at indicated time points and analysed by denaturing PAGE. Data are mean ± SD from three independent reactions. Degradation trajectories of ompD were fitted to one phase exponential decay. Formation and decay of intermediates from ompD -cleavage at position +83 were fitted to two-exponential equation [I = exp(- kt ) – exp(- jt )] with degradation rate k and formation rate j . D Cleavage specificities for nucleolytic processing of site +83 in ompD in the different assembly states, expressed as the formation rate of the +83 intermediate over the degradation rate of the respective ompD fragment starting material. Data are mean ± SD from three independent reactions. E Conformational substates of <t>the</t> <t>TEC-30S</t> IC assembly. F Substate of the early expressome proposed to facilitate the accommodation of Hfq/MicC on the bound ompD mRNA. The colours of the segmented map in ( E ) correspond to the components shown in the schematic.
    Tec 30s Ic Structure, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 197 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    tec 30s ic structure - by Bioz Stars, 2026-02
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    Images

    1) Product Images from "Structure of the 30S translation initiation complex coupled to paused RNA polymerase and its potential for riboregulation"

    Article Title: Structure of the 30S translation initiation complex coupled to paused RNA polymerase and its potential for riboregulation

    Journal: Nature Communications

    doi: 10.1038/s41467-025-67330-2

    A Schematic of the ompD transcript and MicC recognition site. B , C Cleavage time courses of ompD mRNA fragment and +83-cleavage intermediate species (see Fig. and Suppl. Fig. for representative raw data). Free ompD mRNA fragment (black), ompD 89 -TEC (green), ompD 89 -30S IC (grey) and ompD 89 -TEC-IC (red) were incubated with MicC/Hfq and then subjected to cleavage by the RNA degradosome. Reactions were stopped at indicated time points and analysed by denaturing PAGE. Data are mean ± SD from three independent reactions. Degradation trajectories of ompD were fitted to one phase exponential decay. Formation and decay of intermediates from ompD -cleavage at position +83 were fitted to two-exponential equation [I = exp(- kt ) – exp(- jt )] with degradation rate k and formation rate j . D Cleavage specificities for nucleolytic processing of site +83 in ompD in the different assembly states, expressed as the formation rate of the +83 intermediate over the degradation rate of the respective ompD fragment starting material. Data are mean ± SD from three independent reactions. E Conformational substates of the TEC-30S IC assembly. F Substate of the early expressome proposed to facilitate the accommodation of Hfq/MicC on the bound ompD mRNA. The colours of the segmented map in ( E ) correspond to the components shown in the schematic.
    Figure Legend Snippet: A Schematic of the ompD transcript and MicC recognition site. B , C Cleavage time courses of ompD mRNA fragment and +83-cleavage intermediate species (see Fig. and Suppl. Fig. for representative raw data). Free ompD mRNA fragment (black), ompD 89 -TEC (green), ompD 89 -30S IC (grey) and ompD 89 -TEC-IC (red) were incubated with MicC/Hfq and then subjected to cleavage by the RNA degradosome. Reactions were stopped at indicated time points and analysed by denaturing PAGE. Data are mean ± SD from three independent reactions. Degradation trajectories of ompD were fitted to one phase exponential decay. Formation and decay of intermediates from ompD -cleavage at position +83 were fitted to two-exponential equation [I = exp(- kt ) – exp(- jt )] with degradation rate k and formation rate j . D Cleavage specificities for nucleolytic processing of site +83 in ompD in the different assembly states, expressed as the formation rate of the +83 intermediate over the degradation rate of the respective ompD fragment starting material. Data are mean ± SD from three independent reactions. E Conformational substates of the TEC-30S IC assembly. F Substate of the early expressome proposed to facilitate the accommodation of Hfq/MicC on the bound ompD mRNA. The colours of the segmented map in ( E ) correspond to the components shown in the schematic.

    Techniques Used: Incubation



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    A Schematic of the ompD transcript and MicC recognition site. B , C Cleavage time courses of ompD mRNA fragment and +83-cleavage intermediate species (see Fig. and Suppl. Fig. for representative raw data). Free ompD mRNA fragment (black), ompD 89 -TEC (green), ompD 89 -30S IC (grey) and ompD 89 -TEC-IC (red) were incubated with MicC/Hfq and then subjected to cleavage by the RNA degradosome. Reactions were stopped at indicated time points and analysed by denaturing PAGE. Data are mean ± SD from three independent reactions. Degradation trajectories of ompD were fitted to one phase exponential decay. Formation and decay of intermediates from ompD -cleavage at position +83 were fitted to two-exponential equation [I = exp(- kt ) – exp(- jt )] with degradation rate k and formation rate j . D Cleavage specificities for nucleolytic processing of site +83 in ompD in the different assembly states, expressed as the formation rate of the +83 intermediate over the degradation rate of the respective ompD fragment starting material. Data are mean ± SD from three independent reactions. E Conformational substates of <t>the</t> <t>TEC-30S</t> IC assembly. F Substate of the early expressome proposed to facilitate the accommodation of Hfq/MicC on the bound ompD mRNA. The colours of the segmented map in ( E ) correspond to the components shown in the schematic.
    Tec 30s Ic Structure, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    A Schematic of the ompD transcript and MicC recognition site. B , C Cleavage time courses of ompD mRNA fragment and +83-cleavage intermediate species (see Fig. and Suppl. Fig. for representative raw data). Free ompD mRNA fragment (black), ompD 89 -TEC (green), ompD 89 -30S IC (grey) and ompD 89 -TEC-IC (red) were incubated with MicC/Hfq and then subjected to cleavage by the RNA degradosome. Reactions were stopped at indicated time points and analysed by denaturing PAGE. Data are mean ± SD from three independent reactions. Degradation trajectories of ompD were fitted to one phase exponential decay. Formation and decay of intermediates from ompD -cleavage at position +83 were fitted to two-exponential equation [I = exp(- kt ) – exp(- jt )] with degradation rate k and formation rate j . D Cleavage specificities for nucleolytic processing of site +83 in ompD in the different assembly states, expressed as the formation rate of the +83 intermediate over the degradation rate of the respective ompD fragment starting material. Data are mean ± SD from three independent reactions. E Conformational substates of <t>the</t> <t>TEC-30S</t> IC assembly. F Substate of the early expressome proposed to facilitate the accommodation of Hfq/MicC on the bound ompD mRNA. The colours of the segmented map in ( E ) correspond to the components shown in the schematic.
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    A Schematic of the ompD transcript and MicC recognition site. B , C Cleavage time courses of ompD mRNA fragment and +83-cleavage intermediate species (see Fig. and Suppl. Fig. for representative raw data). Free ompD mRNA fragment (black), ompD 89 -TEC (green), ompD 89 -30S IC (grey) and ompD 89 -TEC-IC (red) were incubated with MicC/Hfq and then subjected to cleavage by the RNA degradosome. Reactions were stopped at indicated time points and analysed by denaturing PAGE. Data are mean ± SD from three independent reactions. Degradation trajectories of ompD were fitted to one phase exponential decay. Formation and decay of intermediates from ompD -cleavage at position +83 were fitted to two-exponential equation [I = exp(- kt ) – exp(- jt )] with degradation rate k and formation rate j . D Cleavage specificities for nucleolytic processing of site +83 in ompD in the different assembly states, expressed as the formation rate of the +83 intermediate over the degradation rate of the respective ompD fragment starting material. Data are mean ± SD from three independent reactions. E Conformational substates of <t>the</t> <t>TEC-30S</t> IC assembly. F Substate of the early expressome proposed to facilitate the accommodation of Hfq/MicC on the bound ompD mRNA. The colours of the segmented map in ( E ) correspond to the components shown in the schematic.
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    Image Search Results


    A Schematic of the ompD transcript and MicC recognition site. B , C Cleavage time courses of ompD mRNA fragment and +83-cleavage intermediate species (see Fig. and Suppl. Fig. for representative raw data). Free ompD mRNA fragment (black), ompD 89 -TEC (green), ompD 89 -30S IC (grey) and ompD 89 -TEC-IC (red) were incubated with MicC/Hfq and then subjected to cleavage by the RNA degradosome. Reactions were stopped at indicated time points and analysed by denaturing PAGE. Data are mean ± SD from three independent reactions. Degradation trajectories of ompD were fitted to one phase exponential decay. Formation and decay of intermediates from ompD -cleavage at position +83 were fitted to two-exponential equation [I = exp(- kt ) – exp(- jt )] with degradation rate k and formation rate j . D Cleavage specificities for nucleolytic processing of site +83 in ompD in the different assembly states, expressed as the formation rate of the +83 intermediate over the degradation rate of the respective ompD fragment starting material. Data are mean ± SD from three independent reactions. E Conformational substates of the TEC-30S IC assembly. F Substate of the early expressome proposed to facilitate the accommodation of Hfq/MicC on the bound ompD mRNA. The colours of the segmented map in ( E ) correspond to the components shown in the schematic.

    Journal: Nature Communications

    Article Title: Structure of the 30S translation initiation complex coupled to paused RNA polymerase and its potential for riboregulation

    doi: 10.1038/s41467-025-67330-2

    Figure Lengend Snippet: A Schematic of the ompD transcript and MicC recognition site. B , C Cleavage time courses of ompD mRNA fragment and +83-cleavage intermediate species (see Fig. and Suppl. Fig. for representative raw data). Free ompD mRNA fragment (black), ompD 89 -TEC (green), ompD 89 -30S IC (grey) and ompD 89 -TEC-IC (red) were incubated with MicC/Hfq and then subjected to cleavage by the RNA degradosome. Reactions were stopped at indicated time points and analysed by denaturing PAGE. Data are mean ± SD from three independent reactions. Degradation trajectories of ompD were fitted to one phase exponential decay. Formation and decay of intermediates from ompD -cleavage at position +83 were fitted to two-exponential equation [I = exp(- kt ) – exp(- jt )] with degradation rate k and formation rate j . D Cleavage specificities for nucleolytic processing of site +83 in ompD in the different assembly states, expressed as the formation rate of the +83 intermediate over the degradation rate of the respective ompD fragment starting material. Data are mean ± SD from three independent reactions. E Conformational substates of the TEC-30S IC assembly. F Substate of the early expressome proposed to facilitate the accommodation of Hfq/MicC on the bound ompD mRNA. The colours of the segmented map in ( E ) correspond to the components shown in the schematic.

    Article Snippet: For the coupled TEC-30S IC structure, 12,011 multi-frame movies were then collected on a 300 kV FEI Titan Krios equipped with a Gatan K3 detector.

    Techniques: Incubation