1OIN
Family 1 b-glucosidase from Thermotoga maritima
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-2 |
Synchrotron site | ESRF |
Beamline | ID14-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-12-15 |
Detector | ADSC CCD |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 94.910, 94.980, 113.928 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 * - 2.150 |
R-factor | 0.204 |
Rwork | 0.201 |
R-free | 0.25000 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1od0 |
RMSD bond length | 0.018 |
RMSD bond angle | 1.620 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 * | 2.230 |
High resolution limit [Å] | 2.150 | 2.150 |
Rmerge | 0.057 * | 0.400 * |
Number of reflections | 56583 | |
<I/σ(I)> | 25.56 | 5.14 |
Completeness [%] | 100.0 | 100 |
Redundancy | 5.4 | 5.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7 | 18 * | 10MG/ML PROTEIN IN 15% PEG 4K, 0.2 M CAAC, 0.1M IMIDAZOLE PH7, pH 7.00 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | enzyme | 10 (mg/ml) | |
2 | 1 | drop | imidazole | 50 (mM) | pH7. |
3 | 1 | reservoir | PEG4000 | 15 (%) | |
4 | 1 | reservoir | 0.2 (M) | ||
5 | 1 | reservoir | imidazole | 0.1 (M) | pH7. |