1QMV
thioredoxin peroxidase B from red blood cells
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X11 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1998-07-15 |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 88.880, 107.030, 119.500 |
Unit cell angles | 90.00, 110.87, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.700 |
Rwork | 0.192 |
R-free | 0.25600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1prx |
RMSD bond length | 0.011 |
RMSD bond angle | 0.027 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.730 |
High resolution limit [Å] | 1.700 | 1.700 |
Rmerge | 0.057 * | 0.481 * |
Number of reflections | 228010 | |
<I/σ(I)> | 18.8 | 1.7 |
Completeness [%] | 99.6 | 93.6 |
Redundancy | 4.2 | 2.3 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 | 290 * | drop consists of equal volume of protein and reservoir solutions * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 25 (mM) | |
3 | 1 | drop | EDTA | 5 (mM) | |
4 | 1 | drop | dithiothreitol | 10 (mM) | |
5 | 1 | reservoir | PEG400 | 16 (%(v/v)) | |
6 | 1 | reservoir | Tris-HCl | 100 (mM) | |
7 | 1 | reservoir | 2-propanol | 10 (%(v/v)) | |
8 | 1 | reservoir | dithiothreitol | 10 (mM) |