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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Procapsid of bacteriophage lambda | |||||||||
![]() | Low resolution phage lambda procapsid map. | |||||||||
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Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 8.0 Å | |||||||||
![]() | Maruthi K / Prokhorov NS / Morais MC | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Assembly Incompetent Major Capsid Protein Reveals Elementary and Transient Interactions with Scaffolding Chaparone that Nucleate Viral Shell Assembly Authors: Davis CR / Churchill ME / Backos D / Maruthi K / Prokhorov NS / Morais MC / Catalano CE | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 21.6 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 7.9 KB 7.9 KB | Display Display | ![]() |
Images | ![]() | 265.4 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 324.3 KB | Display | ![]() |
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Full document | ![]() | 323.9 KB | Display | |
Data in XML | ![]() | 7.1 KB | Display | |
Data in CIF | ![]() | 8.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
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Links
EMDB pages | ![]() ![]() |
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Map
File | ![]() | ||||||||||||||||||||
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Annotation | Low resolution phage lambda procapsid map. | ||||||||||||||||||||
Voxel size | X=Y=Z: 2.8 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : Procapsid of bacteriophage lambda
Entire | Name: Procapsid of bacteriophage lambda |
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Components |
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-Supramolecule #1: Procapsid of bacteriophage lambda
Supramolecule | Name: Procapsid of bacteriophage lambda / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Major Capsid Protein
Macromolecule | Name: Major Capsid Protein / type: protein_or_peptide / ID: 1 / Enantiomer: DEXTRO |
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Sequence | String: MSMYTTAQLL AANEQKFKFD PLFLRLFFRE SYPFTTEKVY LSQIPGLVNM ALYVSPIVSG EVIRSRGGS TSEFTPGYVK PKHEVNPQMT LRRLPDEDPQ NLADPAYRRR RIIMQNMRDE E LAIAQVEE MQAVSAVLKG KYTMTGEAFD PVEVDMGRSE ENNITQSGGT ...String: MSMYTTAQLL AANEQKFKFD PLFLRLFFRE SYPFTTEKVY LSQIPGLVNM ALYVSPIVSG EVIRSRGGS TSEFTPGYVK PKHEVNPQMT LRRLPDEDPQ NLADPAYRRR RIIMQNMRDE E LAIAQVEE MQAVSAVLKG KYTMTGEAFD PVEVDMGRSE ENNITQSGGT EWSKRDKSTY DP TDDIEAY ALNASGVVNI IVFDPKGWAL FRSFKAVKEK LDTRRGSNSE LETAVKDLGK AVS YKGMYG DVAIVVYSGQ YVENGVKKNF LPDNTMVLGN TQARGLRTYG CIQDADAQRE GINA SARYP KNWVTTGDPA REFTMIQSAP LMLLADPDEF VSVQLA |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 8 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | JEOL 2200FS |
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Image recording | Film or detector model: DIRECT ELECTRON DE-20 (5k x 3k) / Average electron dose: 30.0 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: ![]() |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD |
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Image processing
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 8.0 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 1253 |
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Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: PROJECTION MATCHING |