+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-23403 | |||||||||
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Title | Reconstituted 207 bp Archaeasome, Class I | |||||||||
Map data | Reconstructed volume of Arc207 complex (Archaeasome complex with 7 archaeal histone dimers binding 207 bp of DNA), Arc150 "base" resolved with unresolved Arc60 "lid". | |||||||||
Sample |
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Biological species | Thermococcus kodakarensis (archaea) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 9.5 Å | |||||||||
Authors | Bowerman S / Luger K | |||||||||
Funding support | United States, 1 items
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Citation | Journal: Elife / Year: 2021 Title: Archaeal chromatin 'slinkies' are inherently dynamic complexes with deflected DNA wrapping pathways. Authors: Samuel Bowerman / Jeff Wereszczynski / Karolin Luger / Abstract: Eukaryotes and many archaea package their DNA with histones. While the four eukaryotic histones wrap ~147 DNA base pairs into nucleosomes, archaeal histones form 'nucleosome-like' complexes that ...Eukaryotes and many archaea package their DNA with histones. While the four eukaryotic histones wrap ~147 DNA base pairs into nucleosomes, archaeal histones form 'nucleosome-like' complexes that continuously wind between 60 and 500 base pairs of DNA ('archaeasomes'), suggested by crystal contacts and analysis of cellular chromatin. Solution structures of large archaeasomes (>90 DNA base pairs) have never been directly observed. Here, we utilize molecular dynamics simulations, analytical ultracentrifugation, and cryoEM to structurally characterize the solution state of archaeasomes on longer DNA. Simulations reveal dynamics of increased accessibility without disruption of DNA-binding or tetramerization interfaces. Mg concentration influences compaction, and cryoEM densities illustrate that DNA is wrapped in consecutive substates arranged 90 out-of-plane with one another. Without ATP-dependent remodelers, archaea may leverage these inherent dynamics to balance chromatin packing and accessibility. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_23403.map.gz | 2.3 MB | EMDB map data format | |
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Header (meta data) | emd-23403-v30.xml emd-23403.xml | 10 KB 10 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_23403_fsc.xml | 11.9 KB | Display | FSC data file |
Images | emd_23403.png | 41.2 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-23403 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-23403 | HTTPS FTP |
-Related structure data
Related structure data | C: citing same article (ref.) |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_23403.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Reconstructed volume of Arc207 complex (Archaeasome complex with 7 archaeal histone dimers binding 207 bp of DNA), Arc150 "base" resolved with unresolved Arc60 "lid". | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.219 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
-Entire : Archaeasome containing 207 bp of DNA
Entire | Name: Archaeasome containing 207 bp of DNA |
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Components |
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-Supramolecule #1: Archaeasome containing 207 bp of DNA
Supramolecule | Name: Archaeasome containing 207 bp of DNA / type: complex / ID: 1 / Parent: 0 Details: Archaeasome (archaeal histone-DNA complex) formed by 7 histone dimers wrapping 207 bp of DNA. |
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Source (natural) | Organism: Thermococcus kodakarensis (archaea) |
Recombinant expression | Organism: Escherichia coli (E. coli) |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Concentration | 0.9 mg/mL | |||||||||
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Buffer | pH: 8 Component:
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Vitrification | Cryogen name: ETHANE / Instrument: HOMEMADE PLUNGER Details: Manual plunge at ambient temperature and humidity.. | |||||||||
Details | Sample was observed to be monodisperse via Sedimentation Velocity Analytical Ultracentrifugation. |
-Electron microscopy
Microscope | FEI TECNAI 20 |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Number grids imaged: 1 / Number real images: 5388 / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD |