4ADC
Structural and functional study of succinyl-ornithine transaminase from E. coli
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-04-07 |
Detector | ADSC QUANTUM 315r |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 184.370, 118.277, 109.457 |
Unit cell angles | 90.00, 96.80, 90.00 |
Refinement procedure
Resolution | 108.690 - 2.300 |
R-factor | 0.1724 |
Rwork | 0.170 |
R-free | 0.21294 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2pb2 |
RMSD bond length | 0.021 |
RMSD bond angle | 2.158 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 19.800 | 2.420 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.100 | 0.340 |
Number of reflections | 101215 | |
<I/σ(I)> | 10.7 | 3 |
Completeness [%] | 97.8 | 86.6 |
Redundancy | 3.5 | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8 | 1.17 M SODIUM MALONATE PH 7.0, 0.09 M TRIS CHLORIDE PH 8.0, 0.02 M DI-ETHYLAMMONIUM FORMATE WITH DRY ORNITHINE POWDER ADDED DIRECTLY TO THE CRYSTAL DROPS. |