9GGI
Crystal structure of argininosuccinate lyase from Arabidopsis thaliana (AtASL)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX IV BEAMLINE BioMAX |
| Synchrotron site | MAX IV |
| Beamline | BioMAX |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2023-05-12 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.976 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 106.044, 229.542, 111.586 |
| Unit cell angles | 90.00, 90.56, 90.00 |
Refinement procedure
| Resolution | 48.450 - 1.550 |
| R-factor | 0.14714 |
| Rwork | 0.147 |
| R-free | 0.17118 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.935 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0425) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.480 | 1.610 |
| High resolution limit [Å] | 1.550 | 1.550 |
| Rmerge | 0.049 | 0.606 |
| Rmeas | 0.061 | 0.775 |
| Number of reflections | 720570 | 73727 |
| <I/σ(I)> | 13 | 1.9 |
| Completeness [%] | 94.1 | 96.4 |
| Redundancy | 2.5 | |
| CC(1/2) | 0.990 | 0.550 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 294 | 0.1M BIS-TRIS pH 5.5, 2.0M Ammonium sulfate |
