ATP-dependent chromatin-remodeling complexes, such as RSC, can reposition, evict 
or restructure nucleosomes. A structure of a RSC-nucleosome complex with a 
nucleosome determined by cryo-EM shows the nucleosome bound in a central RSC 
cavity. Extensive interaction of RSC with histones and DNA seems to destabilize 
the nucleosome and lead to an overall ATP-independent rearrangement of its 
structure. Nucleosomal DNA appears disordered and largely free to bulge out into 
solution as required for remodeling, but the structure of the RSC-nucleosome 
complex indicates that RSC is unlikely to displace the octamer from the 
nucleosome to which it is bound. Consideration of the RSC-nucleosome structure 
and published biochemical information suggests that ATP-dependent DNA 
translocation by RSC may result in the eviction of histone octamers from 
adjacent nucleosomes.