4C5Z
Crystal structure of A. niger ochratoxinase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2011-05-07 |
Detector | DECTRIS PIXEL |
Spacegroup name | P 4 21 2 |
Unit cell lengths | 183.940, 183.940, 79.900 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 73.280 - 2.500 |
R-factor | 0.17704 |
Rwork | 0.175 |
R-free | 0.20890 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | PDB ENTRIES 3BE7 3feq 2R8C 3mtw 2qs8 |
RMSD bond length | 0.011 |
RMSD bond angle | 1.441 |
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] | 92.000 | 2.640 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.180 | 0.610 |
Number of reflections | 46056 | |
<I/σ(I)> | 9.4 | 3.3 |
Completeness [%] | 96.5 | 97.6 |
Redundancy | 9.6 | 9.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8.5 | 10 % (W/V) PEG 3000, 0.1 M TRIS PH 8.5, 0.2 M TRI-POTASSIUM CITRATE |