1CC2
CHOLESTEROL OXIDASE FROM STREPTOMYCES HIS447GLN MUTANT
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 115 |
| Detector technology | IMAGE PLATE |
| Collection date | 1997-12 |
| Detector | RIGAKU RAXIS II |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 51.590, 74.050, 63.800 |
| Unit cell angles | 90.00, 105.11, 90.00 |
Refinement procedure
| Resolution | 6.000 - 2.200 |
| R-factor | 0.147 * |
| Rwork | 0.147 |
| R-free | 0.23500 |
| Structure solution method | OTHER |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.300 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CCP4 |
| Refinement software | X-PLOR (3.843) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 23.600 | 2.280 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.072 * | 0.188 |
| Total number of observations | 43413 * | |
| Number of reflections | 22463 | |
| <I/σ(I)> | 8.9 | 3.5 |
| Completeness [%] | 95.0 | 89.2 |
| Redundancy | 1.9 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7 * | 17 * | CRYSTALLIZATION CONDITIONS: VAPOUR DIFFUSION USING THE HANGING DROP TECHNIQUE, PRECIPITANT CONDITIONS: 10-12% PEG 8000 100MM SODIUM CACODYLATE PH 5.2, 75MM MNSO4 PROTEIN CONCENTRATION 8.5MG/ML |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 8.5 (mg/ml) | |
| 2 | 1 | drop | HEPES | 10 (mM) | |
| 3 | 1 | reservoir | PEG8000 | 10-12 (%(w/v)) | |
| 4 | 1 | reservoir | sodium cacodylate | 100 (mM) | |
| 5 | 1 | reservoir | 75 (mM) |
