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 |
