8R5Q
Structure of apo TDO with a bound inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X06DA |
| Synchrotron site | SLS |
| Beamline | X06DA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2023-09-24 |
| Detector | DECTRIS PILATUS 2M-F |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 91.330, 132.490, 135.570 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 75.750 - 2.620 |
| R-factor | 0.255 |
| Rwork | 0.254 |
| R-free | 0.26740 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.850 |
| Data reduction software | autoPROC |
| Data scaling software | autoPROC |
| Phasing software | PHASER |
| Refinement software | BUSTER (2.11.8) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 94.800 | 2.860 |
| High resolution limit [Å] | 2.620 | 2.620 |
| Rmerge | 0.094 | 1.330 |
| Rpim | 0.101 | |
| Number of reflections | 39729 | 16059 |
| <I/σ(I)> | 14.5 | 1.5 |
| Completeness [%] | 94.8 | 58.3 |
| Redundancy | 6.8 | 6.4 |
| CC(1/2) | 0.610 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 5.3 mg/ml (124 uM) protein containing 2 mM AMT and 1 mM inhibitor, 12.5 % PEG 4000, 20% hexanetriol, 20 mM each of arginine, threonine, histidine, 5-hydroxylysine, trans-4-hydroxy-L-proline, 100 mM AMPD pH 8.5 |
