4BLT
P4 PROTEIN FROM BACTERIOPHAGE PHI12 S292A MUTANT IN COMPLEX WITH AMPcPP
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 |
| Detector | ADSC CCD |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 104.352, 131.727, 159.285 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 38.460 - 2.400 |
| R-factor | 0.26402 |
| Rwork | 0.263 |
| R-free | 0.28977 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1w44 |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.951 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | CNS |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 20.000 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.110 | 0.290 |
| Number of reflections | 40589 | |
| <I/σ(I)> | 17.6 | 4.2 |
| Completeness [%] | 93.1 | 70.7 |
| Redundancy | 9.6 | 6.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 4.8 | 10% PEG 1500 IN 100 MM SODIUM ACETATE PH 4.8 AND 5MM AMCPP |
