Pseudo-atomic model of a fiberless isometric variant of bacteriophage phi29
by single particle (icosahedral) reconstruction, at 7.9 A resolution

#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-1116, Made by Jmol
#6: Superimposing with simplified surface model of EM map, EMDB-1120, Made by Jmol
#7: Superimposing with EM 3D map: EMDB-1120, Made by UCSF CHIMERA
Entry | |
| Summary | |
| Database / ID | PORTEIN DATA BANK (PDB) / 1yxn |
|---|---|
| Title | Pseudo-atomic model of a fiberless isometric variant of bacteriophage phi29 |
| Descriptor | Major head protein |
| Keywords | Virus, phi29, capsid, icosahedral virus capsid, hk97 fold, phage, bacterial immuno-globulin, BIG2, Icosahedral virus |
| Authors | Morais, M.C., Choi, K.H., Koti, J.S., Chipman, P.R., Anderson, D.L., Rossmann, M.G. |
| Date | Deposition: 2005-02-22, Release: 2005-04-26 |
| PDBj Mine pages | Summary, Structural Details, Experimental Details, Functional Details |
| Other databases | RCSB-PDB, PDBe, CATH, CE, FSSP, SCOP, VAST |
| Structure Visualization | |
| Movies | Movie 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-1116, Made by Jmol #6: Superimposing with simplified surface model of EM map, EMDB-1120, Made by Jmol #7: Superimposing with EM 3D map: EMDB-1120, Made by UCSF CHIMERA |
| Structure viewers | Yorodumi, jV4, Jmol, Biological unit (Images, jV) |
| Related Structure Data | |
| Related Entries |
Cite: data citing same article Fit: target map of fitting |
| Similar strucutres (beta) |
List of similar structure data about Omokage system |
Article | |
| Citation - primary | |
| Article | Mol. Cell, Vol. 18, Issue 2, Page 149-59, Year 2005 |
|---|---|
| Title | Conservation of the capsid structure in tailed dsDNA bacteriophages: the pseudoatomic structure of phi29. |
| Authors | Marc C Morais, Kyung H Choi, Jaya S Koti, Paul R Chipman, Dwight L Anderson, Michael G Rossmann Department of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, Indiana 47907, USA. |
| Keywords | Bacillus Phages (chemistry), Capsid (chemistry), Capsid Proteins (chemistry), Cryoelectron Microscopy, DNA, Viral (chemistry), Imaging, Three-Dimensional, Models, Molecular, Models, Structural, Protein Conformation, Protein Structure, Secondary, Protein Structure, Tertiary |
| Links | PII: S1097-2765(05)01183-4, DOI: 10.1016/j.molcel.2005.03.013, PubMed: 15837419 |
Components | |
| ID 1 : Late protein Gp8 | |
| Image | ![]() ![]() |
|---|---|
| Description | Major head protein |
| Type | polymer |
| Formula weight | 30656.020 Da |
| Number of molecules | 3 |
| Source | Method: Isolated from a genetically manipulated source Gene: Phi29-like viruses, phi29, 8, ID:10756, Bacillus phage phi29Host: Bacillus, ID:1423, Bacillus subtilis |
| Links | Sequence view |
Sample | |
| Assembly | |
| Aggregation state | PARTICLE |
|---|---|
| Name | Fiberless isometric phi29 capsid |
| Entity assembly | |
| Details | The virus particle is a protein shell with icosahedral symmetry. To generate the complete icosahedral particle, apply the following 59 matrices to the three chains in the icosahedral asymmetric unit, and combine with the original coordinates of the icosahedral asymmetric unit: |
| Name | The capsid protein assembles a T=3 icosahedral virus shell. |
| Virus entity | |
| Virus host category | Bacteria |
| Virus host growth cell | Bacillus subtilus |
| Virus host species | Bacillus subtilus |
| Virus type | bacteriophage |
| Buffer | |
| Name | tris-HCL |
| Experiment | |
| Reconstruction method | SINGLE PARTICLE |
| Specimen type | VITREOUS ICE (CRYO EM) |
| Sample preparation | |
| pH | 7.8 |
| Sample concentration | 1.0 mg/ml |
| Sample support | |
| Details | electron microscopy grid - in vitreous ice |
| Vitrification | |
| Details | frozen in liquid ethane |
Electron Microscopy | |
| Imaging | |
| Microscope | model: FEI/PHILIPS CM200FEG/ST |
|---|---|
| Electron gun | |
| Electron source | Field emmission gun |
| Accelerating voltage | 200 kV |
| Lens | |
| Magnification | nominal: 38000 X |
| Cs | nominal: 2.0 mm |
| Specimen holder | |
| Tilt angle | min: 0.0 degrees, max: 0.0 degrees |
| Temperature | 100 Kelvin |
| Detector | |
| Type | KODAK SO163 FILM |
Processing | |
| 2D projection selection | |
| Software name | Situs (colores) |
|---|---|
| Single particle entity | |
| Symmetry type | ICOSAHEDRAL |
| 3D reconstruction | |
| CTF correction method | Inverse of CTF was applied to images. Both phases and amplitudes were corrected. |
| Details | Software used included P3DR (3D reconstructions), PFT (initial orientation improvement), and POR (final orientation refinement. |
| Method | 3D reconstructions were calculated using the Fourier-Bessel method. Initial orientations were found via common-lines, improved using model based polar Fourier transform methods, and finally refined by minimizing the vector difference between between structure factors calculated from a particle image and those from a central section of the Fourier transform of the model. |
| Nominal pixel size | 1.8421 A/pix |
| Resolution | 7.9 A |
| 3D fitting | |
| Method | 6D search for each symmetry related molecule in the icosahedral asymmetric unit |
| Refinement Protocol | rigid body |
| Refinement Space | REAL |
| Software name | Situs (colores) |
| Target criteria | rigid body refinement in real space against laplacian filtered EM density, using the program COLORES in the package SITUS. Each molecule in the T=3 asymmetric unit was refined separately. |
| Refine hist | |
| Total atoms | 1080 |
| Protein atoms | 1080 |