1H75
Structural basis for the thioredoxin-like activity profile of the glutaredoxin-like protein NrdH-redoxin from Escherichia coli.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MAX II BEAMLINE I711 |
Synchrotron site | MAX II |
Beamline | I711 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 31.151, 41.346, 58.668 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 25.000 - 1.700 |
R-factor | 0.2 |
Rwork | 0.200 |
R-free | 0.21100 |
Structure solution method | MAD |
RMSD bond length | 0.008 |
RMSD bond angle | 1.310 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | |
High resolution limit [Å] | 1.700 | |
Rmerge | 0.058 | |
Total number of observations | 113655 * | |
Number of reflections | 8503 | |
<I/σ(I)> | 17.5 | |
Completeness [%] | 96.4 | 88.7 * |
Redundancy | 13.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 9.1 | 20 * | pH 9.10 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | CHES | 0.05 (M) | |
2 | 1 | drop | protein | 16 (mg/ml) | |
3 | 1 | reservoir | sodium citrate | 1.20 (M) | |
4 | 1 | reservoir | Tris-HCl | 200 (mM) | |
5 | 1 | reservoir | MPD | 5 (%) |