2VHT
P4 PROTEIN FROM BACTERIOPHAGE PHI12 R279A mutant in complex with ATP
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 | 2007-07-14 |
| Detector | ADSC CCD |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 104.870, 130.947, 158.672 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 101.020 - 3.000 |
| R-factor | 0.249 |
| Rwork | 0.247 |
| R-free | 0.28500 |
| Structure solution method | OTHER |
| Starting model (for MR) | NONE |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.079 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 3.110 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.280 | 0.980 |
| Number of reflections | 22064 | |
| <I/σ(I)> | 6 | 1.5 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 4.6 | 4.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 4.8 | 10% PEG 1500, 100MM NAAC PH 4.8, 5MM ATP |
