4ADB
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 315 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 184.708, 118.428, 109.792 |
Unit cell angles | 90.00, 96.69, 90.00 |
Refinement procedure
Resolution | 109.050 - 2.200 |
R-factor | 0.17323 |
Rwork | 0.171 |
R-free | 0.21885 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2pb2 |
RMSD bond length | 0.021 |
RMSD bond angle | 2.076 |
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 | 2.320 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.130 | 0.610 |
Number of reflections | 118526 | |
<I/σ(I)> | 14.6 | 3.4 |
Completeness [%] | 99.7 | 99 |
Redundancy | 7.6 | 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 IN 150 PLUS 150 NL DROPS. |