1BEA
BIFUNCTIONAL HAGEMAN FACTOR/AMYLASE INHIBITOR FROM MAIZE
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 298 |
Detector technology | IMAGE PLATE |
Collection date | 1995-05 |
Detector | RIGAKU RAXIS IIC |
Spacegroup name | P 42 21 2 |
Unit cell lengths | 57.120, 57.120, 80.240 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 45.000 - 1.950 |
R-factor | 0.195 |
Rwork | 0.195 |
R-free | 0.28700 |
Structure solution method | MIR/MOLECULAR REPLACEMENT |
Starting model (for MR) | 1bip |
RMSD bond length | 0.016 |
RMSD bond angle | 25.200 * |
Data reduction software | PROCESS |
Data scaling software | PROCESS |
Phasing software | EPMR |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 45.000 | 1.970 |
High resolution limit [Å] | 1.950 | 1.940 |
Number of reflections | 9031 | |
Completeness [%] | 92.0 | 65.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 7.5 | PROTEIN WAS CRYSTALLIZED FROM 30% PEG-400, 100 MM HEPES PH 7.5, 0.2 M MGCL2. CRYSTAL WAS SOAKED IN 0.1 M SODIUM ACETATE, 30% PEG-400, 0.2 M MGCL2, PH 5.8 PRIOR TO DATA COLLECTION. |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 25 (mg/ml) | |
2 | 1 | reservoir | PEG400 | 30 (%) | |
3 | 1 | reservoir | 0.2 (M) | ||
4 | 1 | reservoir | HEPES | 0.1 (M) | pH7.5 |