4HBO
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-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 298 |
| Detector technology | CCD |
| Collection date | 2011-10-20 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.979 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 42.790, 279.700, 76.725 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.617 - 3.241 |
| R-factor | 0.3424 |
| Rwork | 0.340 |
| R-free | 0.36790 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4har |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.197 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER (2.3.0) |
| Refinement software | PHENIX (1.8_1069) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 3.310 |
| High resolution limit [Å] | 3.241 | 8.810 | 3.250 |
| Rmerge | 0.107 | 0.061 | 0.522 |
| Number of reflections | 7669 | ||
| <I/σ(I)> | 7.7 | ||
| Completeness [%] | 99.0 | 99.1 | 92.7 |
| Redundancy | 12.7 | 12.3 | 10.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 18% PEG 4000, 20% 2-propanol, 0.1 M Tris, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
