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Figure 2. Two configurations in the ATPγS–CMG–DNA complex.. From: Cryo-EM structures of the eukaryotic replicative helicase bound to a translocation substrate.
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Figure 1. CMG helicase structure at subnanometre resolution.. From: Cryo-EM structures of the eukaryotic replicative helicase bound to a translocation substrate.
Figure 3. The MCM ATPase centres.. From: Cryo-EM structures of the eukaryotic replicative helicase bound to a translocation substrate.
Figure 7. Origin activation and replication fork unwinding by the CMG helicase.. From: Cryo-EM structures of the eukaryotic replicative helicase bound to a translocation substrate.
Figure 4. DNA-bound form of the CMG helicase.. From: Cryo-EM structures of the eukaryotic replicative helicase bound to a translocation substrate.
Figure 5. Comparison of the ATPγS–CMG–DNA structure with available helicase–nucleic acid assemblies.. From: Cryo-EM structures of the eukaryotic replicative helicase bound to a translocation substrate.
Figure 6. DNA engagement and deformation by the CMG helicase.. From: Cryo-EM structures of the eukaryotic replicative helicase bound to a translocation substrate.
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