3EAN
Crystal structure of recombinant rat selenoprotein thioredoxin reductase 1 with reduced 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 | 2007-04-07 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.978 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 78.574, 140.669, 171.167 |
Unit cell angles | 90.00, 94.50, 90.00 |
Refinement procedure
Resolution | 29.740 - 2.750 |
R-factor | 0.20799 |
Rwork | 0.206 |
R-free | 0.23602 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1h6v |
RMSD bond length | 0.015 |
RMSD bond angle | 1.494 |
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] | 84.000 | 2.900 |
High resolution limit [Å] | 2.750 | 2.750 |
Rmerge | 0.077 | 0.400 |
Number of reflections | 95938 | |
<I/σ(I)> | 15.2 | 2.6 |
Completeness [%] | 99.5 | 98.9 |
Redundancy | 3.5 | 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 |