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For many years, biologists have been trying to understand how DNA is packaged into chromosomes. A breakthrough came in the 1970s when it was established that all eukaryotic chromosomes
consist of a regularly repeating protein-DNA complex called the nucleosome1. Each nucleosome consists of a protein octamer, made up of two copies each of histones H2A, H2B, H3 and H4, which,
together with the fifth histone, H1, organizes about 200 base pairs (bp) of DNA. Further organization involves the assembly of nucleosomes into higher-order chromatin structures.
On page 251of this issue, Luger et al.2 report the much awaited high-resolution structure of the nucleosome core particle. This landmark structure confirms many of the expected features of
the nucleosome core. But it also reveals some surprises. Importantly, it provides a structural basis for interpreting the many molecular mechanisms that have evolved to regulate access to
the DNA in chromatin.
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