8R5R
Structure of apo TDO with a bound inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2023-10-09 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 91.738, 132.906, 137.495 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.830 - 3.078 |
| R-factor | 0.228 |
| Rwork | 0.227 |
| R-free | 0.25190 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.820 |
| 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] | 76.310 | 3.240 |
| High resolution limit [Å] | 3.080 | 3.080 |
| Rmerge | 0.171 | |
| Rpim | 0.056 | |
| Number of reflections | 27716 | 1386 |
| <I/σ(I)> | 9.8 | 1.3 |
| Completeness [%] | 95.2 | 60.6 |
| Redundancy | 9.8 | 8.6 |
| CC(1/2) | 0.998 | 0.536 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 5.3 mg/ml (124 uM) protein containing 2 mM AMT and 1 mM inhibitor Reservoir solution: Morpheus II condition F8 5%(w/v) PEG 20K, 25%(w/v) 1,1,1-tris(hydroxymethyl)propane, 1%(w/v) NDSB 195,0.02M of each Monosaccharide II, 0.1M BES/TEA pH 7.5 |
