2VTU
crystal structure of bacteriophage MS2 covalent coat protein dimer
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-4 |
Synchrotron site | ESRF |
Beamline | ID14-4 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-05-19 |
Detector | ADSC CCD |
Spacegroup name | F 4 3 2 |
Unit cell lengths | 220.438, 220.438, 220.438 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.000 - 3.500 |
R-factor | 0.2723 |
Rwork | 0.272 |
R-free | 0.31020 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2ms2 |
RMSD bond length | 0.054 |
RMSD bond angle | 1.700 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 45.000 | 3.630 |
High resolution limit [Å] | 3.500 | 3.500 |
Rmerge | 0.150 | 0.360 |
Number of reflections | 6079 | |
<I/σ(I)> | 17.3 | 6.7 |
Completeness [%] | 97.8 | 99.2 |
Redundancy | 5.6 | 5.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.5 | 0.32M NA2HPO4, 0.08M NAH2PO4 AND 5% PEG 8000, pH 7.5 |