3G1G
Crystal structure of the C-terminal domain from the Rous Sarcoma Virus capsid protein: High pH
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.1 |
| Synchrotron site | ALS |
| Beamline | 8.2.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-05-26 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.0332 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 46.600, 72.200, 48.000 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.970 - 2.010 |
| R-factor | 0.21882 |
| Rwork | 0.217 |
| R-free | 0.25703 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1eoq |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.508 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0044) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.058 | 0.329 |
| Number of reflections | 11209 | |
| <I/σ(I)> | 20.9 | 3.3 |
| Completeness [%] | 99.7 | 100 |
| Redundancy | 3.5 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 10.3 | 291 | 0.2M Beta-Alanine/KOH, pH10.3, 10-25% PEG8000, VAPOR DIFFUSION, SITTING DROP, temperature 291K |
