2C9N
Structure of the Epstein-Barr virus ZEBRA protein at approximately 3. 5 Angstrom resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-3 |
Synchrotron site | ESRF |
Beamline | ID14-3 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-11-06 |
Detector | MARRESEARCH |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 185.300, 36.370, 26.470 |
Unit cell angles | 90.00, 95.25, 90.00 |
Refinement procedure
Resolution | 30.000 - 3.300 |
R-factor | 0.368 |
Rwork | 0.368 |
R-free | 0.36600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2c91 |
RMSD bond length | 0.015 |
RMSD bond angle | 1.900 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 3.400 |
High resolution limit [Å] | 3.300 | 3.300 |
Rmerge | 0.060 | 0.260 |
Number of reflections | 9861 | |
<I/σ(I)> | 15.3 | 5.3 |
Completeness [%] | 98.1 | |
Redundancy | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6 | pH 6.00 |