4HAR
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 | 2012-03-31 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.979 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 147.760, 74.786, 96.075 |
| Unit cell angles | 90.00, 97.53, 90.00 |
Refinement procedure
| Resolution | 47.623 - 2.663 |
| R-factor | 0.1881 |
| Rwork | 0.185 |
| R-free | 0.23040 |
| Structure solution method | SIRAS |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.337 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE (2.13) |
| Refinement software | PHENIX (1.7.3_928) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.710 |
| High resolution limit [Å] | 2.660 | 7.210 | 2.660 |
| Rmerge | 0.143 | 0.080 | 0.428 |
| Number of reflections | 29218 | ||
| <I/σ(I)> | 13 | ||
| Completeness [%] | 98.6 | 100 | 86.9 |
| Redundancy | 6.7 | 7.4 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | 25% PEG 3350, 0.2M Sodium chloride, 1% Lauryldimethylamine-oxide, 0.05M Bis-Tris, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
