1B85
LIGNIN PEROXIDASE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM1A |
Synchrotron site | ESRF |
Beamline | BM1A |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 1998-11-15 |
Detector | MARRESEARCH |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 73.400, 94.400, 230.990 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 12.000 - 1.850 |
R-factor | 0.142 * |
Rwork | 0.142 |
R-free | 0.18100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1b80 |
RMSD bond length | 0.015 |
RMSD bond angle | 0.030 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 12.000 | 1.880 |
High resolution limit [Å] | 1.850 | 1.850 |
Rmerge | 0.056 | 0.245 |
Total number of observations | 392354 * | |
Number of reflections | 62663 | |
<I/σ(I)> | 14.7 | 4.4 |
Completeness [%] | 91.4 | 89.6 |
Redundancy | 6.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6 * | 20 * | pH 4.0 |
Crystallization Reagents
ID | crystal ID | solution ID | reagent name | concentration | details |
1 | 1 | 1 | PEG 6000 | ||
2 | 1 | 1 | ORCINOL |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 8 (mg/ml) | |
2 | 1 | drop | sodium succinate | 10 (mM) | |
3 | 1 | reservoir | PEG6000 | 17 (%(w/v)) |