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quasi-atomic resolution model of bacteriophage PRD1 sus607 mutant, obtained by combined cryo-EM and X-ray crystallography.

by single particle (icosahedral) reconstruction, at 13.3 A resolution

Movie

Orientation:

#1: Biological unit as complete icosahedral assembly, Made by Jmol

#2: Biological unit as icosahedral pentamer, Made by Jmol

#3: Biological unit as icosahedral 23 hexamer, Made by Jmol

#4: Depositted structure unit, Made by Jmol

#5: Superimposing with simplified surface model of EM map, EMDB-1012, Made by Jmol

#6: Superimposing with EM 3D map: EMDB-1012, Made by UCSF CHIMERA

#7: Superimposing with EM 3D map: EMDB-1012, Made by UCSF CHIMERA

Entry
Summary
Database / IDPORTEIN DATA BANK (PDB) / 1gw8
Titlequasi-atomic resolution model of bacteriophage PRD1 sus607 mutant, obtained by combined cryo-EM and X-ray crystallography.
DescriptorMAJOR CAPSID PROTEIN
KeywordsVIRUS/VIRAL PROTEIN, TECTIVIRIDAE, BACTERIOPHAGE PRD1, CRYO- EM, IMAGE RECONSTRUCTION, ICOSAHEDRAL VIRUS, VIRUS-VIRAL PROTEIN complex
AuthorsSan Martin, C., Huiskonen, J.T., Bamford, J.K.H., Butcher, S.J., Fuller, S.D., Bamford, D.H., Burnett, R.M.
DateDeposition: 2002-03-08, Release: 2002-03-15
PDBj Mine pagesSummary, Structural Details, Experimental Details, Functional Details
Other databasesRCSB-PDB, PDBe, CATH, CE, FSSP, SCOP, VAST
Compound detailsBACTERIOPHAGE PRD1 SUS607 MUTANT LACKS THE VIRAL MEMBRANE AGGREGATION PROTEIN P11
Structure Visualization
MoviesMovie Page

#1: Biological unit as complete icosahedral assembly, Made by Jmol

#2: Biological unit as icosahedral pentamer, Made by Jmol

#3: Biological unit as icosahedral 23 hexamer, Made by Jmol

#4: Depositted structure unit, Made by Jmol

#5: Superimposing with simplified surface model of EM map, EMDB-1012, Made by Jmol

#6: Superimposing with EM 3D map: EMDB-1012, Made by UCSF CHIMERA

#7: Superimposing with EM 3D map: EMDB-1012, Made by UCSF CHIMERA

Structure viewersYorodumi, jV4, Jmol, Biological unit (Images, jV)
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EMDB-1012

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Cite: data citing same article

Fit: target map of fitting

Similar strucutres (beta)
List of similar structure data about Omokage system
Article
Citation - primary
ArticleNat. Struct. Biol., Vol. 9, Issue 10, Page 756-63, Year 2002
TitleMinor proteins, mobile arms and membrane-capsid interactions in the bacteriophage PRD1 capsid.
AuthorsCarmen San Martín, Juha T Huiskonen, Jaana K H Bamford, Sarah J Butcher, Stephen D Fuller, Dennis H Bamford, Roger M Burnett
The Wistar Institute, 3601 Spruce Street, Philadelphia, Pennsylvania 19104, USA.
KeywordsBacteriophage PRD1 (genetics), Capsid (metabolism), Cloning, Molecular, Crystallography, X-Ray, Intracellular Membranes (metabolism), Models, Molecular
LinksPubMed: 12219080, DOI: 10.1038/nsb837
Citation - 1
ArticleActa Crystallogr. D Biol. Crystallogr., Vol. 58, Issue Pt 1, Page 39-59, Year 2002
TitleThe X-ray crystal structure of P3, the major coat protein of the lipid-containing bacteriophage PRD1, at 1.65 A resolution.
AuthorsStacy D Benson, Jaana K H Bamford, Dennis H Bamford, Roger M Burnett
The Wistar Institute, 3601 Spruce Street, Philadelphia, PA 19104, USA.
KeywordsBacteriophage PRD1 (chemistry), Capsid (chemistry), Crystallography, X-Ray, Lipids (chemistry), Models, Molecular, Molecular Structure, Virion (chemistry)
LinksPubMed: 11752778
Citation - 2
ArticleStructure, Vol. 9, Issue 10, Page 917-30, Year 2001
TitleCombined EM/X-ray imaging yields a quasi-atomic model of the adenovirus-related bacteriophage PRD1 and shows key capsid and membrane interactions.
AuthorsC S Martín, R M Burnett, F de Haas, R Heinkel, T Rutten, S D Fuller, S J Butcher, D H Bamford
The Wistar Institute, 3601 Spruce Street, Philadelphia, PA 19104, USA.
KeywordsAdenoviruses, Human (chemistry), Bacteriophage PRD1 (chemistry), Capsid (chemistry), Computer Simulation, Cryoelectron Microscopy (methods), Crystallography, X-Ray (methods), DNA, Viral (chemistry), Image Enhancement (methods), Models, Molecular, Protein Conformation, Viral Envelope Proteins (chemistry), Virion (chemistry)
LinksPubMed: 11591347, PII: S0969212601006426
Citation - 3
ArticleCell, Vol. 98, Issue 6, Page 825-33, Year 1999
TitleViral evolution revealed by bacteriophage PRD1 and human adenovirus coat protein structures.
AuthorsS D Benson, J K Bamford, D H Bamford, R M Burnett
The Wistar Institute, Philadelphia, Pennsylvania 19104, USA.
KeywordsAdenoviruses, Human (chemistry), Amino Acid Sequence, Capsid (chemistry), Capsid Proteins, Crystallization, Crystallography, X-Ray, Evolution, Molecular, Models, Molecular, Molecular Sequence Data, Protein Conformation, Synchrotrons, Tectiviridae (chemistry), hexon capsid protein, Adenovirus, protein P3, bacteriophage PRD1
LinksPubMed: 10499799, PII: S0092-8674(00)81516-0
Components
ID 1 : PROTEIN P3
Image
DescriptionMAJOR CAPSID PROTEIN
Typepolymer
Formula weight43346.695 Da
Number of molecules12
DetailsSUS607 MUTANT LACKS THE VIRAL MEMBRANE AGGREGATION PROTEIN P11
SourceMethod: Isolated from a genetically manipulated source
Gene: ID:10658, BACTERIOPHAGE PRD1
Host: ID:602, SALMONELLA TYPHIMURIUM, DS88
Plasmid name: PSN3
LinksUniProt: P22535, Sequence view
Sample
Assembly
Aggregation statePARTICLE
NameBACTERIOPHAGE PRD1 SUS607
Buffer
NameTRIS
Experiment
Reconstruction methodSINGLE PARTICLE
Specimen typeVITREOUS ICE (CRYO EM)
Sample preparation
pH7.2
Sample support
DetailsHOLEY CARBON
Vitrification
DetailsETHANE
Electron Microscopy
Imaging
Microscopemodel: FEI CM200 FEG
Date2001-12-01
Electron gun
Electron sourceFEG
Accelerating voltage200 kV
Illumination modeLOW DOSE
Lens
Magnificationcalibrated: 45100 X, nominal: 50000 X
Csnominal: 2 mm
Nominal defocusmax: 4100 nm, min: 1300 nm
Specimen holder
Temperature95 Kelvin
Detector
TypeKODAK SO-163 FILM
Image scans
Number digital images21
Processing
2D projection selection
Number of particles569
Software nameSPIDER, MRC_ICOS
Single particle entity
Symmetry typeICOSAHEDRAL
3D reconstruction
Actual pixel size3.32 A/pix
CTF correction methodPHASE RESTORATION BY CTF- MULTIPLICATION OF IMAGES; AMPLITUDE RESTORATION BY COMPARISON WITH QUASI- ATOMIC MODEL
DetailsRIGID BODY REFINEMENT AGAINST CRYO-EM MAP XPLOR 3.851 (BRUNGER). DATA USED IN REFINEMENT. RESOLUTION RANGE HIGH INFINITY RESOLUTION RANGE LOW 15A DATA CUTOFF (SIGMA(F)) 0.0 NUMBER OF REFLECTIONS 1430672 FIT TO DATA USED IN
Magnification calibrationCOMPARISON WITH X- RAY DATA
MethodPOLAR FOURIER TRANSFORM, CROSS- COMMON LINES
Nominal pixel size3.68 A/pix
Resolution13.3 A
3D fitting
MethodRIGID BODY
Refinement ProtocolX-RAY
Refinement SpaceRECIPROCAL
Target criteriaR-FACTOR
3D fitting list
PDB entry ID1HX6
Refine
Ls d res high13.30 A
ID1
Refine hist
D res high13.30
Total atoms34170
Protein atoms34170
Download
PDB format
Allpdb1gw8.ent.gz
pdb1gw8.ent (uncompressed file)
Header onlypdb1gw8.ent.gz
mmCIF format
mmCIF1gw8.cif.gz
XML format
All1gw8.xml.gz
No-atom1gw8-noatom.xml.gz
Ext-atom1gw8-extatom.xml.gz
Movie files
movie #1
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movie #7
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