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-Structure paper
Title | Histones with an unconventional DNA-binding mode in vitro are major chromatin constituents in the bacterium Bdellovibrio bacteriovorus. |
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Journal, issue, pages | Nat Microbiol, Vol. 8, Page 2006-2019, Year 2023 |
Publish date | Jan 19, 2023 (structure data deposition date) |
Authors | Hocher, A. / Laursen, S.P. / Radford, P. / Tyson, J. / Lambert, C. / Stevens, K.M. / Montoya, A. / Shliaha, P.V. / Picardeau, M. / Sockett, R.E. ...Hocher, A. / Laursen, S.P. / Radford, P. / Tyson, J. / Lambert, C. / Stevens, K.M. / Montoya, A. / Shliaha, P.V. / Picardeau, M. / Sockett, R.E. / Luger, K. / Warnecke, T. |
External links | Nat Microbiol / PubMed:37814071 |
Methods | X-ray diffraction |
Resolution | 1.8 - 2 Å |
Structure data | PDB-8fvx: PDB-8fw7: |
Chemicals | ChemComp-HOH: |
Source |
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Keywords | DNA BINDING PROTEIN / Histone / NAP / DNA BINDING PROTEIN/DNA / nucleosome / scaffold / DNA BINDING PROTEIN-DNA complex |