5NII
Crystal structure of the atypical thioredoxin reductase TRi from Desulfovibrio vulgaris Hildenborough
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2013-12-07 |
| Detector | DECTRIS PILATUS3 S 6M |
| Wavelength(s) | 0.97625 |
| Spacegroup name | I 2 2 2 |
| Unit cell lengths | 66.387, 148.161, 152.886 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.480 - 2.000 |
| R-factor | 0.1961 |
| Rwork | 0.194 |
| R-free | 0.22820 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3fd8 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.289 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 47.480 |
| High resolution limit [Å] | 2.000 |
| Number of reflections | 92563 |
| <I/σ(I)> | 16.24 |
| Completeness [%] | 99.2 |
| Redundancy | 3.67 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 | 12% PEG 3350, 100 mM BisTris pH 6.0 |
