Major studies have been made in the understanding of nucleosome structure and function over the years. Co-crystallization and comprehensive NMR analysis of chromatin factors and the nucleosome core particle have established the acidic patch arginine-anchor as a paradigm for nucleosome recognition. Advancements in cryo-EM technology have aided in the visualization of the two-start 30 nm fiber and characterization of nucleosome binding by large and conformationally flexible chromatin enzymes. More recently, Tosi and colleagues used cryo-EM and cross-linking mass spectrometry (XL-MS) to extensively characterize the interaction of the holo-INO80 complex with the nucleosome core particle (NCP). NCP bound cryo-EM reconstitutions have also been reported for the Saccharomyces cerevisiae Piccolo NuA4 histone acetyltransferase (HAT) complex and the HP1-like heterochromatin protein Swi6 from Schizosaccharomyces pombe.
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