1B4V
CHOLESTEROL OXIDASE FROM STREPTOMYCES
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 115 |
Detector technology | IMAGE PLATE |
Collection date | 1996-10-01 |
Detector | RIGAKU RAXIS II |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 51.304, 72.964, 63.022 |
Unit cell angles | 90.00, 105.09, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.500 |
R-factor | 0.181 |
Rwork | 0.181 |
R-free | 0.20000 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3cox |
RMSD bond length | 0.006 |
RMSD bond angle | 1.400 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | X-PLOR (3.843) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 22.300 | 1.550 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.045 | 0.220 |
Total number of observations | 402969 * | |
Number of reflections | 62747 | |
<I/σ(I)> | 27.5 | 2 |
Completeness [%] | 87.4 | 30.9 |
Redundancy | 6.4 | 0.31 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 * | 17 * | PRECIPITANT CONDITIONS: 10- 12% PEG 8000, 100MM SODIUM CACODYLATE PH 5.2, 75MM MNSO4 PROTEIN CONCENTRATION 8.5MG/ML, VAPOR DIFFUSION, HANGING DROP |
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) |