2VHC
P4 PROTEIN FROM BACTERIOPHAGE PHI12 N234G mutant in complex with AMPCPP and MN
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-07-27 |
Detector | MARRESEARCH |
Spacegroup name | I 2 2 2 |
Unit cell lengths | 105.120, 129.518, 158.522 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 100.500 - 2.350 |
R-factor | 0.177 |
Rwork | 0.174 |
R-free | 0.23700 |
Structure solution method | OTHER |
Starting model (for MR) | NONE |
RMSD bond length | 0.012 |
RMSD bond angle | 1.383 |
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 | 2.430 |
High resolution limit [Å] | 2.350 | 2.350 |
Rmerge | 0.100 | 0.380 |
Number of reflections | 45742 | |
<I/σ(I)> | 27 | 5 |
Completeness [%] | 100.0 | 99 |
Redundancy | 11.1 | 9.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 4.8 | 10% PEG 1500, 100MM NAAC PH 4.8, 5MM AMPCPP, 5MM MNCL |