1QO4
ARABIDOPSIS THALIANA PEROXIDASE A2 AT ROOM TEMPERATURE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 287 |
Detector technology | IMAGE PLATE |
Collection date | 1999-08-15 |
Detector | RIGAKU IMAGE PLATE |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 46.290, 74.848, 80.794 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 3.000 |
R-factor | 0.183 |
Rwork | 0.183 |
R-free | 0.23500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1pa2 |
RMSD bond length | 0.008 |
RMSD bond angle | 21.300 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS (0.5) |
Refinement software | CNS (0.5) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 * | 3.100 |
High resolution limit [Å] | 3.000 | 3.000 |
Rmerge | 0.165 * | 0.295 * |
Total number of observations | 27478 * | |
Number of reflections | 5887 | |
<I/σ(I)> | 8 | 5 |
Completeness [%] | 97.8 * | 97.3 |
Redundancy | 4.6 | 3.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.5 | Ostergaard, L., (2000) Plant Mol. Biol., 44, 231. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 0.98 (mg/ml) | |
2 | 1 | drop | 0.1 (M) | ||
3 | 1 | drop | cacodylate | 0.5 (M) | |
4 | 1 | drop | PEG8000 | 10 (%(w/v)) | |
5 | 1 | reservoir | 0.2 (M) | ||
6 | 1 | reservoir | cacodylate | 0.1 (M) | |
7 | 1 | reservoir | PEG8000 | 20 (%(w/v)) |