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DNA is packaged into the eukaryotic nucleus with a group of proteins that collectively make up the chromatin fiber. All cellular processes that use DNA as a substrate must contend with this higher order packaging of DNA into chromatin in order to gain access to a particular DNA sequence. Chromatin can exist in various dynamic 'states' of compaction that can differ in their degree of accessibility to cellular factors. Euchromatin is characteristically decondensed and accessible, whereas heterochromatin is highly condensed and inaccessible. We are interested in understanding the cellular mechanisms that regulate the interconversions between chromatin states. The histone proteins play an essential role in this process, and are targeted by a diverse array of post-translational modifications that are correlated with distinct chromatin states - leading to the 'histone code' hypothesis. We are combining structural biology and biochemistry to understand how histone post-translational modifications participate in the regulation of chromatin structure.