31LC
X-ray structure of Thioredoxin reductase (TrxR) from Burkholderia cenocepacia (Bc-TrxR)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ELETTRA BEAMLINE 11.2C |
| Synchrotron site | ELETTRA |
| Beamline | 11.2C |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2024-11-19 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 68.290, 68.290, 131.350 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 59.140 - 2.520 |
| Rwork | 0.260 |
| R-free | 0.36570 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.654 |
| Data reduction software | autoPROC |
| Data scaling software | autoPROC |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0430) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 59.140 | 2.360 |
| High resolution limit [Å] | 2.320 | 2.320 |
| Rmerge | 0.074 | 6.382 |
| Number of reflections | 15470 | 795 |
| <I/σ(I)> | 22.6 | 0.6 |
| Completeness [%] | 96.8 | 100 |
| Redundancy | 18.5 | 19.3 |
| CC(1/2) | 1.000 | 0.600 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 298 | 2.0 M ammonium sulphate, 0.1M Tris-HCl pH 8.5 |
