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 |