9UPQ
Structure of 3-amino-3-carboxyltransferase
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-1A |
| Synchrotron site | Photon Factory |
| Beamline | BL-1A |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2023-12-26 |
| Detector | DECTRIS EIGER X 4M |
| Wavelength(s) | 1.02 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 46.710, 91.874, 130.790 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 45.940 - 1.750 |
| R-factor | 0.1781 |
| Rwork | 0.176 |
| R-free | 0.22240 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | AlphaFold |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.974 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.710 | 1.780 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.075 | |
| Number of reflections | 57752 | 3146 |
| <I/σ(I)> | 15.8 | 2 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 7.6 | 7.5 |
| CC(1/2) | 0.999 | 0.741 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 20% (w/v) PEG3350, 200 mM Ammonium nitrate pH6.3 |
