2WIO
Structure of the histidine tagged, open cytochrome P450 Eryk from S. erythraea
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 | 2005-02-17 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 37.932, 57.341, 179.557 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 89.800 - 2.000 |
| R-factor | 0.18587 |
| Rwork | 0.183 |
| R-free | 0.23202 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1oxa |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.543 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.000 | 2.100 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.190 | 0.440 |
| Number of reflections | 22549 | |
| <I/σ(I)> | 10.9 | 3.1 |
| Completeness [%] | 82.2 | 85.9 |
| Redundancy | 4.8 | 4.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8 | 25% PEG3350, 0.2M NACL, 0.1M TRIS PH 8.0 |
