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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-9018 | |||||||||
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Title | DHF79 filament | |||||||||
![]() | DHF79 filament | |||||||||
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![]() | Protein design / filament / PROTEIN FIBRIL | |||||||||
Biological species | synthetic construct (others) | |||||||||
Method | helical reconstruction / cryo EM / Resolution: 6.9 Å | |||||||||
![]() | Lynch EM / Shen H | |||||||||
![]() | ![]() Title: De novo design of self-assembling helical protein filaments. Authors: Hao Shen / Jorge A Fallas / Eric Lynch / William Sheffler / Bradley Parry / Nicholas Jannetty / Justin Decarreau / Michael Wagenbach / Juan Jesus Vicente / Jiajun Chen / Lei Wang / Quinton ...Authors: Hao Shen / Jorge A Fallas / Eric Lynch / William Sheffler / Bradley Parry / Nicholas Jannetty / Justin Decarreau / Michael Wagenbach / Juan Jesus Vicente / Jiajun Chen / Lei Wang / Quinton Dowling / Gustav Oberdorfer / Lance Stewart / Linda Wordeman / James De Yoreo / Christine Jacobs-Wagner / Justin Kollman / David Baker / ![]() ![]() Abstract: We describe a general computational approach to designing self-assembling helical filaments from monomeric proteins and use this approach to design proteins that assemble into micrometer-scale ...We describe a general computational approach to designing self-assembling helical filaments from monomeric proteins and use this approach to design proteins that assemble into micrometer-scale filaments with a wide range of geometries in vivo and in vitro. Cryo-electron microscopy structures of six designs are close to the computational design models. The filament building blocks are idealized repeat proteins, and thus the diameter of the filaments can be systematically tuned by varying the number of repeat units. The assembly and disassembly of the filaments can be controlled by engineered anchor and capping units built from monomers lacking one of the interaction surfaces. The ability to generate dynamic, highly ordered structures that span micrometers from protein monomers opens up possibilities for the fabrication of new multiscale metamaterials. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 7.2 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 11.5 KB 11.5 KB | Display Display | ![]() |
Images | ![]() | 104.7 KB | ||
Filedesc metadata | ![]() | 5.1 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6e9vMC ![]() 9016C ![]() 9017C ![]() 9019C ![]() 9020C ![]() 9021C ![]() 6e9rC ![]() 6e9tC ![]() 6e9xC ![]() 6e9yC ![]() 6e9zC C: citing same article ( M: atomic model generated by this map |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | DHF79 filament | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.26 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : DHF79 filament
Entire | Name: DHF79 filament |
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Components |
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-Supramolecule #1: DHF79 filament
Supramolecule | Name: DHF79 filament / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: synthetic construct (others) |
-Macromolecule #1: DHF79 filament
Macromolecule | Name: DHF79 filament / type: protein_or_peptide / ID: 1 / Number of copies: 26 / Enantiomer: LEVO |
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Source (natural) | Organism: synthetic construct (others) |
Molecular weight | Theoretical: 23.111928 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: PEDELKRVEK LVKEAEMLLM LAKIKGSEKD LEKALRTAEE AAREAKKVLE QAEKEGDPEV ALRAVELVVR VAELLLRIAK ESGSEEALM TALLVAVVAA TLAVRVLVLA AVQGDPEVAL RAVELVVRVA ELLLRIAKES GSEEALERAL RVAEEAARLA K RVLELAQE ...String: PEDELKRVEK LVKEAEMLLM LAKIKGSEKD LEKALRTAEE AAREAKKVLE QAEKEGDPEV ALRAVELVVR VAELLLRIAK ESGSEEALM TALLVAVVAA TLAVRVLVLA AVQGDPEVAL RAVELVVRVA ELLLRIAKES GSEEALERAL RVAEEAARLA K RVLELAQE QGDPVVAIAA VMLVKRVAEL LERIARESGS EEAKERAERV REE |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | helical reconstruction |
Aggregation state | filament |
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Sample preparation
Buffer | pH: 8 |
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Grid | Details: unspecified |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TECNAI F20 |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Average electron dose: 45.0 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | ![]() Model: Tecnai F20 / Image courtesy: FEI Company |
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Image processing
Final reconstruction | Applied symmetry - Helical parameters - Δz: 5.07952 Å Applied symmetry - Helical parameters - Δ&Phi: 77.6764 ° Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric) Resolution.type: BY AUTHOR / Resolution: 6.9 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 32583 |
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Startup model | Type of model: OTHER / Details: Cylinder |
Final angle assignment | Type: NOT APPLICABLE / Software - Name: RELION |
-Atomic model buiding 1
Refinement | Protocol: RIGID BODY FIT |
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Output model | ![]() PDB-6e9v: |