3F6N
Crystal structure of the virion-associated protein P3 from Caulimovirus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-2 |
Synchrotron site | ESRF |
Beamline | ID23-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-02-15 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 0.931 |
Spacegroup name | P 64 |
Unit cell lengths | 104.943, 104.943, 72.527 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.850 - 3.100 |
R-factor | 0.229 |
Rwork | 0.222 |
R-free | 0.28700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1t6f |
RMSD bond length | 0.008 |
RMSD bond angle | 1.037 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0053) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 3.270 |
High resolution limit [Å] | 3.100 | 3.100 |
Rmerge | 0.065 | 0.306 |
Number of reflections | 8369 | |
<I/σ(I)> | 16.5 | 4.6 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 5.4 | 5.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 291 | 25% PEG 1000, 0.1M MES-NaOH buffer, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 291.0K |