4C60
Crystal structure of A. niger ochratoxinase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2011-07-14 |
| Detector | DECTRIS PILATUS 6M |
| Spacegroup name | I 1 2 1 |
| Unit cell lengths | 212.671, 79.920, 218.280 |
| Unit cell angles | 90.00, 105.25, 90.00 |
Refinement procedure
| Resolution | 74.470 - 2.500 |
| R-factor | 0.20705 |
| Rwork | 0.206 |
| R-free | 0.23054 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4c5z |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.342 |
| Data reduction software | iMOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 74.700 | 2.640 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.100 | 0.360 |
| Number of reflections | 111178 | |
| <I/σ(I)> | 5.7 | 2.1 |
| Completeness [%] | 91.0 | 70.5 |
| Redundancy | 2.5 | 1.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5 | 11% (W/V) PEG 3000, 0.1 M CITRATE PH 5.0, 0.2 M TRI-POTASSIUM CITRATE |
