ISIS Neutron and Muon Source Data Journal

Interaction of the intrinsically-disordered linker histone C-terminal tail with DNA.

Abstract: In cells, the genome needs to be tightly packaged in the nucleus as "chromatin" while still allowing access to the cellular machinery responsible for gene expression. The first level of packaging involves the "core histone” proteins, which form spools around which two turns of DNA are wrapped, a series of which gives rise to an array resembling "beads on a string". This is further condensed by "linker histone" proteins, one of which binds to each spool, arranging them into a thicker fibre. The precise way in which this is accomplished is, despite decades of research, still a hotly debated topic since linker histones have long tails that do not have a static defined 3D structure even when bound to the linker DNA that they are directly responsible for condensing, thus conventional diffraction-based methods fail. We aim to use SANS for this important piece of the chromatin structure puzzle.

Principal Investigator: Dr Katherine Stott
Experimenter: Dr Matthew Watson
Experimenter: Dr Najet Mahmoudi

DOI: 10.5286/ISIS.E.RB1720381

ISIS Experiment Number: RB1720381

Publisher: STFC ISIS Neutron and Muon Source

Data format: RAW/Nexus
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Data Citation

The recommended format for citing this dataset in a research publication is as:
[author], [date], [title], [publisher], [doi]

For Example:
Dr Katherine Stott et al; (2017): Interaction of the intrinsically-disordered linker histone C-terminal tail with DNA., STFC ISIS Neutron and Muon Source, https://doi.org/10.5286/ISIS.E.RB1720381

Data is released under the CC-BY-4.0 license.