ArticleBiochemistry and biophysics reports2015
Solution structure of variant H2A.Z.1 nucleosome investigated by small-angle X-ray and neutron scatterings.
Article in Biochemistry and biophysics reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- Integrated analysis with iCM-SANS, SAXS and MD simulations for dynamics of multi-domain proteins.Journal of applied crystallography · 2026Article
- Solution conformational differences between conventional and CENP-A nucleosomes are accentuated by reversible deformation under high pressure.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2025Article
- Small-angle neutron scattering contrast variation studies of biological complexes: Challenges and triumphs.Current opinion in structural biology · 2022Review
- Apolipoprotein E Binding Drives Structural and Compositional Rearrangement of mRNA-Containing Lipid Nanoparticles.ACS nano · 2021Article
- Examining Membrane Proteins by Neutron Scattering.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Biochemical characterization of the placeholder nucleosome for DNA hypomethylation maintenance.Biochemistry and biophysics reports · 2019Article
- Nucleosome structure and dynamics are coming of age.Nature structural & molecular biology · 2019Review
- Identification of the amino acid residues responsible for stable nucleosome formation by histone H3.Y.Nucleus (Austin, Tex.) · 2017Article
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Solution structures of nucleosomes containing a human histone variant, H2A.Z.1, were measured by small-angle X-ray and neutron scatterings (SAXS and SANS). SAXS revealed that the outer shape, reflecting the DNA shape, of the H2A.Z.1 nucleosome is almost the same as that of the canonical H2A nucleosome. In contrast, SANS employing a contrast variation technique revealed that the histone octamer of the H2A.Z.1 nucleosome is smaller than that of the canonical nucleosome. The DNA within the H2A.Z.1 nucleosome was more susceptible to micrococcal nuclease than that within the canonical nucleosome. These results suggested that the DNA is loosely wrapped around the histone core in the H2A.Z.1 nucleosome.
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