2C9L
Structure of the Epstein-Barr virus ZEBRA protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID13 |
| Synchrotron site | ESRF |
| Beamline | ID13 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-09-11 |
| Detector | MARRESEARCH |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 94.170, 26.520, 98.090 |
| Unit cell angles | 90.00, 103.95, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.250 |
| R-factor | 0.2317 |
| Rwork | 0.232 |
| R-free | 0.26440 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ysa |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.200 |
| 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 | 2.300 |
| High resolution limit [Å] | 2.250 | 2.250 |
| Rmerge | 0.090 | 0.450 |
| Number of reflections | 11609 | |
| <I/σ(I)> | 11.1 | 4.4 |
| Completeness [%] | 99.8 | 99.9 |
| Redundancy | 5.3 | 5.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7 | pH 7.00 |
