4ADE
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 | 2011-04-12 |
Detector | ADSC QUANTUM 315 |
Spacegroup name | H 3 2 |
Unit cell lengths | 231.469, 231.469, 110.416 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 115.730 - 2.750 |
R-factor | 0.15633 |
Rwork | 0.154 |
R-free | 0.20133 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2pb2 |
RMSD bond length | 0.017 |
RMSD bond angle | 1.803 |
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] | 19.900 | 2.900 |
High resolution limit [Å] | 2.750 | 2.750 |
Rmerge | 0.150 | 0.720 |
Number of reflections | 29220 | |
<I/σ(I)> | 21.9 | 6 |
Completeness [%] | 99.3 | 99.2 |
Redundancy | 22.1 | 22.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 5 | 293 | 1.4 M SODIUM MALONATE PH 7, 10% (V/V) MMT (MALATE-MES-TRIS) BUFFER AT PH 5.0, AT 293K WITH A PROTEIN TO CRYSTALLANT RATIO OF 3:1 IN THE PRESENCE OF SILVER BULLET SCREEN NUMBER 62. |