4ADD
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 | 2011-06-14 |
| Detector | ADSC QUANTUM 315 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 183.938, 118.264, 109.238 |
| Unit cell angles | 90.00, 96.82, 90.00 |
Refinement procedure
| Resolution | 108.460 - 2.450 |
| R-factor | 0.17303 |
| Rwork | 0.170 |
| R-free | 0.22534 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PREVIOUSLY-DETERMINED NATIVE |
| RMSD bond length | 0.018 |
| RMSD bond angle | 2.095 |
| 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 | 2.580 |
| High resolution limit [Å] | 2.450 | 2.450 |
| Rmerge | 0.150 | 0.630 |
| Number of reflections | 85143 | |
| <I/σ(I)> | 10.6 | 2.9 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 5.9 | 5.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 9 | 293 | 1.5 M AMMONIUM SULFATE, 10% (V/V) MMT (MALATE-MES-TRIS) BUFFER AT PH 9.0, 293K, 150 PLUS 150 NL DROPS. PROTEIN HAD PLP AND SUCCINYLORNITHINE PREVIOUSLY ADDED. |
