2I9F
Structure of the equine arterivirus nucleocapsid protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 200 |
Detector technology | CCD |
Collection date | 2006-05-18 |
Detector | MAR CCD 165 mm |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 68.230, 73.230, 138.960 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 49.940 - 2.000 |
R-factor | 0.21866 |
Rwork | 0.217 |
R-free | 0.24753 |
Structure solution method | SAD |
RMSD bond length | 0.018 |
RMSD bond angle | 1.623 |
Data reduction software | DENZO |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | DM |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 49.940 | 2.060 |
High resolution limit [Å] | 1.950 | 1.950 |
Rmerge | 0.079 | 0.525 |
Number of reflections | 25482 | |
<I/σ(I)> | 28.9 | 7 |
Completeness [%] | 99.1 | 98.2 |
Redundancy | 19.5 | 19.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 311 | 0.1M sodium phosphate, 25% PEG 3350, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 311K |