9IVE
Structure of wild-type aminotransferase from Mycolicibacterium neoaurum in complex with LLP and ALA
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRF BEAMLINE BL19U1 |
| Synchrotron site | SSRF |
| Beamline | BL19U1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2022-09-03 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9785 |
| Spacegroup name | P 1 |
| Unit cell lengths | 66.927, 78.806, 92.094 |
| Unit cell angles | 96.84, 108.76, 112.90 |
Refinement procedure
| Resolution | 35.940 - 1.930 |
| R-factor | 0.1836 |
| Rwork | 0.182 |
| R-free | 0.21510 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.750 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.21_5207: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 35.940 | 2.000 |
| High resolution limit [Å] | 1.930 | 1.930 |
| Rmerge | 0.440 | |
| Rpim | 0.277 | |
| Number of reflections | 111972 | 16244 |
| <I/σ(I)> | 2.43 | |
| Completeness [%] | 94.9 | |
| Redundancy | 3.8 | |
| CC(1/2) | 0.998 | 0.835 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 298 | 0.1 M Sodium Cacodylate pH 6.5,0.2 M MgCl2,10 %PEG 3000 |
