Fig. 5: Structural plasticity of MuV helical nucleocapsids. | Communications Biology

Fig. 5: Structural plasticity of MuV helical nucleocapsids.

From: Structural plasticity of mumps virus nucleocapsids with cryo-EM structures

Fig. 5

a, b Structural comparison among Nring-stacked, NChelix-dense, and NChelix-hyper. The helical axis for each structure is set upright (a). One protomer from NChelix-dense or NChelix-hyper is superimposed with one from Nring-stacked, and the angles of helical axes between NChelix-dense and Nring-stacked as well as between NChelix-hyper and Nring-stacked are labeled (b). c Diagrams of filament assembly of NChelix-dense and NChelix-hyper after the superimposition with Nring-stacked. The helical axis for Nring-stacked is set upright. Distance between neighboring protomers and helical rises is marked. d The SDS-PAGE gel (left) and RNA gel (middle) of aged MuV nucleoproteins and a representative cryo-EM image of aged MuV nucleoproteins (right). e Genome condensation from NChelix-dense to NChelix-hyper. The heights of 390-nt RNA in NChelix-dense and NChelix-hyper are marked.

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