4AEC
Crystal Structure of the Arabidopsis thaliana O-Acetyl-Serine-(Thiol)- Lyase C
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC QUANTUM 315r |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 65.390, 65.390, 293.050 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.940 - 2.400 |
R-factor | 0.18306 |
Rwork | 0.180 |
R-free | 0.23315 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1z7w |
RMSD bond length | 0.017 |
RMSD bond angle | 1.735 |
Phasing software | PHASER |
Refinement software | REFMAC (5.4.0078) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.500 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.090 | 0.540 |
Number of reflections | 24684 | |
<I/σ(I)> | 26.1 | 6.3 |
Completeness [%] | 99.7 | 99.6 |
Redundancy | 15.5 | 15.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 291 | 18C, 1:1 15MG/ML PROTEIN MIXED WITH: 28% PEG 8000 100 MM MES, PH 6.5 300 MM NA ACETATE SUPPLEMENTED BY 15% GLYCEROL |