7TJM
Bacteriophage Q beta capsid protein in T3 symmetry
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2021-11-29 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.979 |
| Spacegroup name | H 3 |
| Unit cell lengths | 286.627, 286.627, 662.678 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 49.560 - 3.540 |
| R-factor | 0.2806 |
| Rwork | 0.278 |
| R-free | 0.32780 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1qbe |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.975 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 49.560 | 3.620 |
| High resolution limit [Å] | 3.540 | 3.540 |
| Rmerge | 0.150 | |
| Number of reflections | 247697 | 17430 |
| <I/σ(I)> | 6.4 | |
| Completeness [%] | 99.9 | |
| Redundancy | 10 | |
| CC(1/2) | 0.800 | 0.150 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 8.5 | 298 | PEG 3350, cobalt chloride, Tris |






