2NVK
Crystal Structure of Thioredoxin Reductase from Drosophila melanogaster
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 104 |
Detector technology | IMAGE PLATE |
Collection date | 2006-05-18 |
Detector | MAR scanner 345 mm plate |
Wavelength(s) | 1.5418 |
Spacegroup name | H 3 2 |
Unit cell lengths | 151.487, 151.487, 134.259 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 15.000 - 2.400 |
R-factor | 0.203 |
Rwork | 0.198 |
R-free | 0.24700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1h6v |
RMSD bond length | 0.011 |
RMSD bond angle | 1.359 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 2.490 |
High resolution limit [Å] | 2.400 | 2.400 |
Number of reflections | 22987 | |
<I/σ(I)> | 13.2 | 2.78 |
Completeness [%] | 98.7 | 90.3 |
Redundancy | 7.85 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 293 | 200 mM Succinate, 22% PEG 6000, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |