2CL4
Ascorbate Peroxidase R172A mutant
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-3 |
| Synchrotron site | ESRF |
| Beamline | ID14-3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-08-02 |
| Detector | ADSC CCD |
| Spacegroup name | P 42 21 2 |
| Unit cell lengths | 81.656, 81.656, 75.056 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 19.800 - 1.800 |
| R-factor | 0.162 |
| Rwork | 0.160 |
| R-free | 0.19900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1oag |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.145 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 28.900 | 1.900 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.070 | 0.300 |
| Number of reflections | 23768 | |
| <I/σ(I)> | 15 | 3 |
| Completeness [%] | 98.9 | 99 |
| Redundancy | 7.05 | 6.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 2.25M LI2SO4, 0.1M HEPES PH8.3 |
