3G21
Crystal structure of the C-terminal domain of the Rous Sarcoma Virus capsid protein: Low pH
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL9-2 |
| Synchrotron site | SSRL |
| Beamline | BL9-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-04-28 |
| Detector | MARMOSAIC 325 mm CCD |
| Wavelength(s) | 0.85503 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 32.179, 32.179, 113.875 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 27.000 - 0.900 |
| R-factor | 0.124 |
| Rwork | 0.124 |
| R-free | 0.14200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3g1g |
| RMSD bond length | 0.018 |
| RMSD bond angle | 0.035 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | SHELX |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 27.000 | 0.930 |
| High resolution limit [Å] | 0.900 | 0.900 |
| Rmerge | 0.058 | 0.167 |
| Number of reflections | 46299 | |
| <I/σ(I)> | 36.2 | 7.2 |
| Completeness [%] | 89.0 | 30 |
| Redundancy | 11.1 | 1.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.3 | 291 | 0.20M Succinic acid/KOH, pH4.3, 13-18% PEG8000, 0.75M Magnesium Nitrate, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
