1O6E
Epstein-Barr virus protease
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 | 2001-06-15 |
| Detector | ADSC CCD |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 52.800, 52.800, 330.500 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 42.000 - 2.300 |
| R-factor | 0.197 |
| Rwork | 0.197 |
| R-free | 0.27300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1fl1 |
| RMSD bond length | 0.010 |
| RMSD bond angle | 24.200 * |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 45.200 | 2.380 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.081 | 0.319 |
| Number of reflections | 132854 | |
| <I/σ(I)> | 5.2 | 2.3 |
| Completeness [%] | 98.1 | 89.9 |
| Redundancy | 5.4 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 * | HANGING DROP METHOD USING A RESERVOIR SOLUTION OF 1.25 - 1.5 M SODIUM FORMATE,100 MM SODIUM CITRATE PH4.6 5 MM EDTA, PROTEIN IN 100 MM NACL 20 MM THRIS-HCL PH 7.5 1 MM EDTA 10 MM BETA-MERCAPTOETHANOL |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 15-21 (mg/ml) | |
| 2 | 1 | drop | 100 (mM) | ||
| 3 | 1 | drop | Tris-HCl | 200 (mM) | pH7.5 |
| 4 | 1 | drop | EDTA | 1 (mM) | |
| 5 | 1 | drop | beta-mercaptoethanol | 10 (mM) | |
| 6 | 1 | drop | DFP | 10 (mM) | |
| 7 | 1 | reservoir | sodium formate | 1.25-1.5 (M) | |
| 8 | 1 | reservoir | sodium citrate | 100 (mM) | or acetate, pH4.6 |
| 9 | 1 | reservoir | EDTA | 5 (mM) |
