Combined with the data showing that the analogous section of BRG1 has histone binding properties, the second proposed model, where the SnAC domain acts as a histone anchor required for remodeling and directly binds to a location on the histone surface, was pursued. This was supported by Fe-BABE targeted cleavage that showed a cleavage site located within the SnAC domain as well as crosslinking data that showed there was a 2-3 fold reduction of Snf2 crosslinking upon deletion of the SnAC domain [62]. In order to find which histones SnAC binds to specifically and the regions of the histone(s) involved, a recombinant SnAC domain protein was generated and used in pull down assays with histones H2A, H3, and H4 in order to show binding and specificity. Finally gH3, a tailless histone H3, was purified to determine if the interaction between the SnAC domain and the histone occurred in either the tail, or core domain of the protein.

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