+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-15146 | ||||||||||||||||||||||||
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Title | H1-bound palindromic nucleosome, state 2 | ||||||||||||||||||||||||
Map data | |||||||||||||||||||||||||
Sample |
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Biological species | Homo sapiens (human) / Xenopus laevis (African clawed frog) | ||||||||||||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 10.0 Å | ||||||||||||||||||||||||
Authors | Alegrio Louro J / Beinsteiner B / Cheng TC / Patel AKM / Boopathi R / Angelov D / Hamiche A / Bednar J / Kale S / Dimitrov S / Klaholz B | ||||||||||||||||||||||||
Funding support | France, European Union, 7 items
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Citation | Journal: Structure / Year: 2023 Title: Nucleosome dyad determines the H1 C-terminus collapse on distinct DNA arms. Authors: Jaime Alegrio Louro / Ramachandran Boopathi / Brice Beinsteiner / Abdul Kareem Mohideen Patel / Tat Cheung Cheng / Dimitar Angelov / Ali Hamiche / Jan Bendar / Seyit Kale / Bruno P Klaholz / Stefan Dimitrov / Abstract: Nucleosomes are symmetric structures. However, binding of linker histones generates an inherently asymmetric H1-nucleosome complex, and whether this asymmetry is transmitted to the overall nucleosome ...Nucleosomes are symmetric structures. However, binding of linker histones generates an inherently asymmetric H1-nucleosome complex, and whether this asymmetry is transmitted to the overall nucleosome structure, and therefore also to chromatin, is unclear. Efforts to investigate potential asymmetry due to H1s have been hampered by the DNA sequence, which naturally differs in each gyre. To overcome this issue, we designed and analyzed by cryo-EM a nucleosome reconstituted with a palindromic (601L) 197-bp DNA. As in the non-palindromic 601 sequence, H1 restricts linker DNA flexibility but reveals partial asymmetrical unwrapping. However, in contrast to the non-palindromic nucleosome, in the palindromic nucleosome H1 CTD collapses to the proximal linker. Molecular dynamics simulations show that this could be dictated by a slightly tilted orientation of the globular domain (GD) of H1, which could be linked to the DNA sequence of the nucleosome dyad. | ||||||||||||||||||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_15146.map.gz | 4.5 MB | EMDB map data format | |
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Header (meta data) | emd-15146-v30.xml emd-15146.xml | 20.2 KB 20.2 KB | Display Display | EMDB header |
Images | emd_15146.png | 92.5 KB | ||
Others | emd_15146_half_map_1.map.gz emd_15146_half_map_2.map.gz | 31.4 MB 31.3 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-15146 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-15146 | HTTPS FTP |
-Validation report
Summary document | emd_15146_validation.pdf.gz | 660.1 KB | Display | EMDB validaton report |
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Full document | emd_15146_full_validation.pdf.gz | 659.7 KB | Display | |
Data in XML | emd_15146_validation.xml.gz | 11.3 KB | Display | |
Data in CIF | emd_15146_validation.cif.gz | 13.2 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-15146 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-15146 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_15146.map.gz / Format: CCP4 / Size: 40.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.055 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_15146_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_15146_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : 197-bp H1-bound palindromic nucleosome
Entire | Name: 197-bp H1-bound palindromic nucleosome |
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Components |
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-Supramolecule #1: 197-bp H1-bound palindromic nucleosome
Supramolecule | Name: 197-bp H1-bound palindromic nucleosome / type: complex / ID: 1 / Chimera: Yes / Parent: 0 / Macromolecule list: #1-#10 Details: 601L nucleosome with 25-bp sequence symmetric linkers and bound to linker histone H1 |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 120 KDa |
-Supramolecule #2: Histone H1.0-B
Supramolecule | Name: Histone H1.0-B / type: complex / ID: 2 / Chimera: Yes / Parent: 1 / Macromolecule list: #3 |
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Source (natural) | Organism: Xenopus laevis (African clawed frog) |
-Supramolecule #3: Core histone octamer
Supramolecule | Name: Core histone octamer / type: complex / ID: 3 / Chimera: Yes / Parent: 1 / Macromolecule list: #4-#10 |
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-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.6 Component:
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Specialist optics | Phase plate: VOLTA PHASE PLATE |
Image recording | #0 - Image recording ID: 1 / #0 - Film or detector model: GATAN K2 SUMMIT (4k x 4k) / #0 - Detector mode: SUPER-RESOLUTION / #0 - Number grids imaged: 1 / #0 - Number real images: 3999 / #0 - Average exposure time: 10.0 sec. / #0 - Average electron dose: 49.0 e/Å2 / #1 - Image recording ID: 2 / #1 - Film or detector model: GATAN K2 SUMMIT (4k x 4k) / #1 - Detector mode: SUPER-RESOLUTION / #1 - Number grids imaged: 1 / #1 - Number real images: 4891 / #1 - Average exposure time: 5.5 sec. / #1 - Average electron dose: 40.7 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 0.01 mm / Nominal defocus max: 1.0 µm / Nominal defocus min: 0.5 µm |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |