4HBE
Crystal Structure of Rubella virus capsid protein (residues 127-277)
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] | 298 |
| Detector technology | CCD |
| Collection date | 2011-06-25 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.006 |
| Spacegroup name | P 2 21 21 |
| Unit cell lengths | 37.730, 71.484, 79.048 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 37.730 - 2.300 |
| R-factor | 0.2054 |
| Rwork | 0.199 |
| R-free | 0.25800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4har |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.230 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER (2.4.0) |
| Refinement software | PHENIX (1.7.3_928) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.320 |
| High resolution limit [Å] | 2.280 | 6.190 | 2.280 |
| Rmerge | 0.113 | 0.082 | 0.441 |
| Number of reflections | 10303 | ||
| <I/σ(I)> | 12.3 | ||
| Completeness [%] | 99.5 | 95.6 | 99.4 |
| Redundancy | 8.1 | 7.4 | 8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 25% PEG 4000, 24% 2-propanol, 0.05M Tris, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
