4PH0
capsid protein from bovine leukemia virus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SOLEIL BEAMLINE PROXIMA 1 |
Synchrotron site | SOLEIL |
Beamline | PROXIMA 1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2013-11-23 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.97857 |
Spacegroup name | P 65 |
Unit cell lengths | 94.280, 94.280, 257.250 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 47.140 - 2.750 |
R-factor | 0.1871 |
Rwork | 0.180 |
R-free | 0.22130 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.009 |
RMSD bond angle | 1.362 |
Data scaling software | XDS |
Refinement software | PHENIX ((phenix.refine: 1.8.4_1496)) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 47.140 | 2.920 | |
High resolution limit [Å] | 2.750 | 8.140 | 2.750 |
Rmerge | 0.067 | 0.026 | 1.015 |
Rmeas | 0.070 | 0.028 | 1.068 |
Total number of observations | 351378 | ||
Number of reflections | 33567 | 1320 | 5374 |
<I/σ(I)> | 22.42 | 77.49 | 2.05 |
Completeness [%] | 99.9 | 98.7 | 99.5 |
Redundancy | 10.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 20mM Tris.HCl, 130mM NaCl, 25% PEG 4000 |