4AON
Conformational dynamics of aspartate alpha-decarboxylase active site revealed by protein-ligand complexes: 1-methyl-L-aspartate complex
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I24 |
Synchrotron site | Diamond |
Beamline | I24 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2011-02-07 |
Detector | DECTRIS PILATUS 6M |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 71.022, 71.022, 216.376 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 61.510 - 1.500 |
R-factor | 0.136 |
Rwork | 0.135 |
R-free | 0.16200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1aw8 |
RMSD bond length | 0.029 |
RMSD bond angle | 2.510 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | MOLREP |
Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 59.160 | 1.580 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.050 | 0.520 |
Number of reflections | 52794 | |
<I/σ(I)> | 33.8 | 6.2 |
Completeness [%] | 99.8 | 98.6 |
Redundancy | 19 | 18.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 4.2 | 5 MG/ML ASPARTATE-ALPHA-DECARBOXYLASE IN 1.5 M AMMONIUM SULFATE, 0.1 M SODIUM CITRATE, PH 3.8 |