2CH8
Structure of the Epstein-Barr Virus Oncogene BARF1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-08-04 |
| Detector | ADSC CCD |
| Spacegroup name | H 3 |
| Unit cell lengths | 179.245, 179.245, 95.720 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.000 - 2.300 |
| R-factor | 0.177 |
| Rwork | 0.174 |
| R-free | 0.23300 |
| Structure solution method | SIRAS |
| RMSD bond length | 0.022 |
| RMSD bond angle | 2.201 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.420 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.060 | 0.230 |
| Number of reflections | 50910 | |
| <I/σ(I)> | 10.7 | 3.1 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 5.3 | 4.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6 | 1 M AMMONIUM SULPHATE,1-2 % PEG 3350,100 MM BISTRIS/HCL PH 6.0 |
