Abstract
Nuclear pore complexes (NPCs) fuse the inner and outer nuclear membranes and mediatenucleocytoplasmic exchange. They are made of 30 different nucleoporins that form an intricatecylindrical architecture around an aqueous central channel. This architecture is highly dynamic inspace and time. Variations in NPC diameter were reported, but the physiological circumstances andthe molecular details remain unknown. Here we combined cryo-electron tomography andsubtomogram averaging with integrative structural modeling to capture a molecular movie of therespective large-scale conformational changes in cellulo.
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