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Yorodumi- EMDB-33199: Cryo-EM structure of the tubular assembly of WGA protein without ... -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-33199 | |||||||||
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Title | Cryo-EM structure of the tubular assembly of WGA protein without symmetry imposition | |||||||||
Map data | cryo-EM map of wheat germ agglutinin protein tube witout symmetry imposition | |||||||||
Sample |
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Keywords | protein tube / self-assembly / carbohydrate interaction / PLANT PROTEIN | |||||||||
Biological species | Triticum aestivum (bread wheat) | |||||||||
Method | helical reconstruction / cryo EM / Resolution: 15.2 Å | |||||||||
Authors | Zhang L / Chen SY / Liu RY | |||||||||
Funding support | China, 1 items
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Citation | Journal: ACS Nano / Year: 2023 Title: Evolution of Protein Assemblies Driven by the Switching of Interplay Mode. Authors: Rongying Liu / Long Li / Shuyu Chen / Zhiwei Yang / Zdravko Kochovski / Shilin Mei / Yan Lu / Lei Zhang / Guosong Chen / Abstract: A protein assembly with the ability to switch interplay modes of multiple driving forces has been achieved. Although biomolecular systems driven by multiple driving forces have been exploited, work ...A protein assembly with the ability to switch interplay modes of multiple driving forces has been achieved. Although biomolecular systems driven by multiple driving forces have been exploited, work on such a protein assembly capable of switching the interplay modes at nanoscale has been rarely reported so far as a result of their great fabrication challenge. In this work, two sets of driving forces such as ligand-ligand interaction and protein-protein interaction were leveraged to antagonistically underpin the multilayered stackings and trigger the hollow evolution to afford the well-defined hollow rectangular frame of proteins. While these protein frames further collapsed into aggregates, the ligand-ligand interactions were weakened, and the interplay of two sets of driving forces thereby tended to switch into synergistic mode, converting the protein packing mode from porously loose packing to axially dense packing and thus giving rise to a morphological evolution toward a nanosized protein tube. This strategy not only provides a nanoscale understanding on the mechanism underlying the switch of interplay modes in the context of biomacromolecules but also may provide access for diverse sophisticated biomacromolecular nanostructures that are historically inaccessible for conventional self-assembly strategies. | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_33199.map.gz | 27.6 MB | EMDB map data format | |
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Header (meta data) | emd-33199-v30.xml emd-33199.xml | 12 KB 12 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_33199_fsc.xml | 7.3 KB | Display | FSC data file |
Images | emd_33199.png | 73.2 KB | ||
Others | emd_33199_half_map_1.map.gz emd_33199_half_map_2.map.gz | 23.4 MB 23.4 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-33199 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-33199 | HTTPS FTP |
-Validation report
Summary document | emd_33199_validation.pdf.gz | 812.8 KB | Display | EMDB validaton report |
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Full document | emd_33199_full_validation.pdf.gz | 812.4 KB | Display | |
Data in XML | emd_33199_validation.xml.gz | 12.8 KB | Display | |
Data in CIF | emd_33199_validation.cif.gz | 17.7 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-33199 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-33199 | HTTPS FTP |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_33199.map.gz / Format: CCP4 / Size: 30.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||
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Annotation | cryo-EM map of wheat germ agglutinin protein tube witout symmetry imposition | ||||||||||||||||||||
Voxel size | X=Y=Z: 2.051 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: EM half map of wheat germ agglutinin protein tube
File | emd_33199_half_map_1.map | ||||||||||||
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Annotation | EM half map of wheat germ agglutinin protein tube | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: EM half map of wheat germ agglutinin protein tube
File | emd_33199_half_map_2.map | ||||||||||||
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Annotation | EM half map of wheat germ agglutinin protein tube | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Helical complex of wheat germ agglutinin protein with R-SL ligand
Entire | Name: Helical complex of wheat germ agglutinin protein with R-SL ligand |
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Components |
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-Supramolecule #1: Helical complex of wheat germ agglutinin protein with R-SL ligand
Supramolecule | Name: Helical complex of wheat germ agglutinin protein with R-SL ligand type: complex / ID: 1 / Parent: 0 |
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Source (natural) | Organism: Triticum aestivum (bread wheat) |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | helical reconstruction |
Aggregation state | helical array |
-Sample preparation
Buffer | pH: 8.5 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TALOS ARCTICA |
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Image recording | Film or detector model: FEI CETA (4k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.5 µm |
Experimental equipment | Model: Talos Arctica / Image courtesy: FEI Company |