4A5G
Raphanus sativus anionic peroxidase.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X6A |
| Synchrotron site | NSLS |
| Beamline | X6A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-03-20 |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 59.148, 41.192, 137.796 |
| Unit cell angles | 90.00, 96.91, 90.00 |
Refinement procedure
| Resolution | 35.287 - 2.050 |
| R-factor | 0.164 |
| Rwork | 0.163 |
| R-free | 0.18520 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1pa2 |
| RMSD bond length | 0.033 |
| RMSD bond angle | 1.727 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.090 |
| High resolution limit [Å] | 1.900 | 2.050 |
| Rmerge | 0.080 | 0.500 |
| Number of reflections | 51917 | |
| <I/σ(I)> | 21.6 | 3.53 |
| Completeness [%] | 98.6 | 99.2 |
| Redundancy | 6.1 | 6.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6.5 | THE PROTEIN CONCENTRATION WAS 50 MG/ML. THE PRECIPITANT SOLUTION COMPRISES 20% PEG 6000, 20% PEG 200, 100 MM MES PH 6.5. |
