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. |