1IZE
Crystal structure of Aspergillus oryzae Aspartic proteinase complexed with pepstatin
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Collection date | 2002-06-03 |
Detector | RIGAKU RAXIS IIC |
Wavelength(s) | 1.5418 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 106.767, 38.627, 78.732 |
Unit cell angles | 90.00, 120.31, 90.00 |
Refinement procedure
Resolution | 52.300 - 1.900 |
R-factor | 0.185 |
Rwork | 0.185 |
R-free | 0.22100 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.005 |
RMSD bond angle | 26.400 * |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 52.340 | 2.020 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.092 | 0.199 * |
Total number of observations | 58695 * | |
Number of reflections | 19551 * | |
Completeness [%] | 100.0 | 75.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 5 | 298 | PEG4000, ammonium acetate, sodium acetate trihydrate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 15 (mg/ml) | |
2 | 1 | reservoir | PEG4000 | 30 (%(w/v)) | |
3 | 1 | reservoir | ammonium acetate | 200 (mM) | |
4 | 1 | reservoir | sodium acetate trihydrate | 100 (mM) | pH5.0 |