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 |