1J1I
Crystal structure of a His-tagged Serine Hydrolase Involved in the Carbazole Degradation (CarC enzyme)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU ULTRAX 18 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2000-12-14 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.5418 |
Spacegroup name | I 4 2 2 |
Unit cell lengths | 130.268, 130.268, 84.491 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 32.570 - 1.860 |
R-factor | 0.215 |
Rwork | 0.215 |
R-free | 0.24800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1iup |
RMSD bond length | 0.006 |
RMSD bond angle | 22.800 * |
Data reduction software | CrystalClear (1.3) |
Data scaling software | CrystalClear (V. 1.3 (MSC/RIGAKU)) |
Phasing software | MOLREP |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 33.220 | 1.930 |
High resolution limit [Å] | 1.860 | 1.860 |
Rmerge | 0.073 | 0.286 |
Number of reflections | 30496 | |
<I/σ(I)> | 6.8 | 2.4 |
Completeness [%] | 99.2 | 98.6 |
Redundancy | 4.6 | 4.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 | 20 * | PEG 6000, citrate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG6000 | 5.2 (%) | |
2 | 1 | reservoir | citric acid | 26 (mM) | pH5.0 |
3 | 1 | drop | protein | 15-20 (mg/ml) |