3EAO
Crystal structure of recombinant rat selenoprotein thioredoxin reductase 1 with oxidized C-terminal tail
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I911-3 |
| Synchrotron site | MAX II |
| Beamline | I911-3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-11-06 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.908 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 78.231, 137.754, 168.954 |
| Unit cell angles | 90.00, 94.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 3.100 |
| R-factor | 0.25806 |
| Rwork | 0.256 |
| R-free | 0.28873 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3ean |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.558 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 64.000 | 3.270 |
| High resolution limit [Å] | 3.100 | 3.101 |
| Rmerge | 0.131 | 0.559 |
| Number of reflections | 64804 | |
| <I/σ(I)> | 10.9 | 1.9 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 3.3 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 0.1M HEPES, PEG 3350 15%, 12% of ethylene glycol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
