4A0R
Structure of bifunctional DAPA aminotransferase-DTB synthetase from Arabidopsis thaliana bound to dethiobiotin (DTB).
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 | CCD |
Detector | ADSC QUANTUM 210 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 246.670, 76.630, 79.840 |
Unit cell angles | 90.00, 108.02, 90.00 |
Refinement procedure
Resolution | 40.436 - 2.680 |
R-factor | 0.1881 |
Rwork | 0.184 |
R-free | 0.25900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | NATIVE DETHIOBIOTIN SYNTHETASE- DIAMINOPELARGONIC ACID AMINOTRANSFERASE FROM ARABIDOPSIS THALIANA |
RMSD bond length | 0.009 |
RMSD bond angle | 1.253 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.440 | 2.750 |
High resolution limit [Å] | 2.680 | 2.680 |
Rmerge | 0.150 | 0.760 |
Number of reflections | 40026 | |
<I/σ(I)> | 9.95 | 1.83 |
Completeness [%] | 99.7 | 99.8 |
Redundancy | 4.2 | 4.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 0.2 M AMMONIUM TARTRATE PH 6.2, 15 % PEG 3350. |