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 |