Data underlying the research on binding of archaeal histones HMfA and HMfB to DNA.

These data were obtained in studies on hypernucleosome formation, an apparently endless nucleosome, by archaeal histones HMfA and HMfB from M. fervidus. Using tethered particle motion and magnetic tweezers the structural, mechanical as well as topological properties were investigated. In addition to the wild type proteins, derivatives mutated at residues proposed to be involved in 'stacking' interactions between layers of the hypernucleosome, were investigated; the data confirmed the importance of these residues.