Related Figures
Figure 7 DNA-crosslinking to PspF1–275 is depende...
Figure 3. PspF1–275 F85Y is the only F85 variant i...
Figure 7. Crosslinking profiles of PspF1–275·σ54·D...
Figure 5. PspF1–275 is similarly organized in all ...
Fig. 5 The activities of the V132A and L138A va...
Figure 1. The cryo-electron microscopy structure o...
Figure 6. Determinants in PspF1–275 required for f...
Fig. 4 Gel filtration profiles of PspF1−275 (WT...
Figure 4. PspF1–275:ADP–BeF alters the σ54–DNA int...
Figure 2. PspF1–275:ADP–BeF supports stable trappe...
Figure 4.: σ54 variants which cannot bind PspF1–275 normally in the presence of ADP·AlFx. ADP·AlFx dependent complexes formed between σ54 and PspF1–275 were detected by Coomassie staining. σ54 and PspF1–275 were presented at 1 and 20 μM separately. Arrow (a) indicates the complex formed between σ54 and PspF1–275 in the presence of ADP·AlFx. Arrow (b) indicates the changed position of PspF1–275 complex in the presence of ADP·AlFx. Arrow (c) and (d) indicates the new bands formed in this assay.
Image Text (High Precision): 1-275 111 PspF
Other Images from "Construction and functional analyses of a comprehensive σ54 site-directed mutant library using alanine–cysteine mutagenesis":
Figure 5. (A) S. meliloti nifH heteroduplex promot...
Figure 7. The left panel shows the cryo-EM reconst...
Figure 3. Formation of holoenzyme by σ54 variants ...
Figure 4. σ54 variants which cannot bind PspF1–275...
Figure 2. In vivo stability of σ54 variants which ...
Figure 6. Mutations in σ54 that affect transcripti...
Figure 1. Diagram of the functional regions of σ54...