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.<br>

本数据集源自针对激烈热球菌（M. fervidus）来源的古菌组蛋白（archaeal histones）HMfA与HMfB所介导的超核小体（hypernucleosome）组装研究，该类超核小体呈现出近似无限延伸的核小体结构。研究人员借助束缚粒子运动（tethered particle motion）与磁镊（magnetic tweezers）技术，对该组装体的结构、力学及拓扑学特性进行了探究。除野生型蛋白外，本研究同时针对被认为参与超核小体层间“堆叠”相互作用的残基所构建的突变体衍生物开展了实验分析；所得数据证实了上述残基的关键作用。