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Found in all eukaryotic cells, linker histones H1 are known to bind to andrearrange nucleosomal linker DNA. In vitro, the fundamental nature of H1/DNAinteractions has attracted wide interest among research communities - forbiologists from a chromatin organization deciphering point of view, and forphysicists from the study of polyelectrolyte interactions point of view. Hence,H1/DNA binding processes, structural and dynamical information about theseself-assemblies is of broad importance. Targeting a quantitative understandingof H1 induced DNA compaction mechanisms our strategy is based on using smallangle X-ray microdiffraction in combination with microfluidics. The usage ofmicrofluidic hydrodynamic focusing devices facilitate a microscale control ofthese self-assembly processes. In addition, the method enables time-resolvedaccess to structure formation in situ, in particular to transient intermediatestates. The observed time dependent structure evolution shows that theinteraction of H1 with DNA can be described as a two step process: an initialunspecific binding of H1 to DNA is followed by a rearrangement of moleculeswithin the formed assemblies. The second step is most likely induced byinteractions between the charged side chains of the protein and DNA. This leadsto an increase in lattice spacing within the DNA/protein assembly and induces adecrease in the correlation length of the mesophases, probably due to a localbending of the DNA.

Structural and dynamic properties of linker histone H1 binding to DNA