2W4B
Epstein-Barr virus alkaline nuclease D203S mutant
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-2 |
| Synchrotron site | ESRF |
| Beamline | ID23-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-08-23 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 87.510, 63.787, 114.131 |
| Unit cell angles | 90.00, 93.59, 90.00 |
Refinement procedure
| Resolution | 31.190 - 3.500 |
| R-factor | 0.19312 |
| Rwork | 0.190 |
| R-free | 0.25550 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2w45 |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.915 |
| Data reduction software | MOSFLM |
| Data scaling software | TRUNCATE |
| Refinement software | REFMAC (5.5.0038) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.990 | 3.530 |
| High resolution limit [Å] | 3.500 | 3.500 |
| Rmerge | 0.090 | 0.170 |
| Number of reflections | 13276 | |
| <I/σ(I)> | 8.53 | 4.02 |
| Completeness [%] | 86.0 | 88.9 |
| Redundancy | 1.92 | 1.87 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | PROTEIN AT 4.5 MG/ML IN 250 MM NACL, 20MM TRIS PH 7.5, RESERVOIR: 10 MM DTT, 10 MM MGCL2, 0.1M HEPES PH 7.0, 1.5% PEG 400 |
