28MB
Structure of Human Aldehyde oxidase under TCEP-reducing conditions
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE MASSIF-3 |
| Synchrotron site | ESRF |
| Beamline | MASSIF-3 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2025-05-12 |
| Detector | DECTRIS EIGER X 4M |
| Wavelength(s) | 0.96770 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 191.204, 273.118, 77.883 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 95.602 - 2.307 |
| Rwork | 0.209 |
| R-free | 0.24090 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.003 |
| RMSD bond angle | 1.029 |
| Data reduction software | XDS |
| Data scaling software | STARANISO |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0425) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 95.790 | 2.600 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 1.400 | |
| Rmeas | 0.350 | |
| Number of reflections | 100292 | 5015 |
| <I/σ(I)> | 6.6 | |
| Completeness [%] | 94.5 | 81.4 |
| Redundancy | 7.1 | |
| CC(1/2) | 1.000 | 0.500 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.7 | 277 | 12% PEG 3350, 100 mM sodium malonate pH 4.7 |
