4BLS
P4 PROTEIN FROM BACTERIOPHAGE PHI12 Q278A 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 QUANTUM 315r |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 105.631, 132.328, 159.938 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.600 |
R-factor | 0.25746 |
Rwork | 0.257 |
R-free | 0.27431 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1w44 |
RMSD bond length | 0.005 |
RMSD bond angle | 1.024 |
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] | 20.000 | 2.690 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.150 | 0.280 |
Number of reflections | 32832 | |
<I/σ(I)> | 7.1 | 7.1 |
Completeness [%] | 94.6 | 93.4 |
Redundancy | 6.6 | 4.8 |
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 |