1BVN
PIG PANCREATIC ALPHA-AMYLASE IN COMPLEX WITH THE PROTEINACEOUS INHIBITOR TENDAMISTAT
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 275 |
Detector technology | FILM |
Detector | KODAK |
Spacegroup name | P 65 2 2 |
Unit cell lengths | 77.700, 77.700, 359.500 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 29.400 - 2.500 |
R-factor | 0.166 |
Rwork | 0.166 |
R-free | 0.26000 |
Structure solution method | MIR |
RMSD bond length | 0.008 |
RMSD bond angle | 27.510 * |
Data reduction software | PROTEIN |
Data scaling software | PROTEIN |
Phasing software | PROTEIN |
Refinement software | X-PLOR (3.185) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.390 | 2.610 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.060 | 0.352 * |
Total number of observations | 54641 * | |
Number of reflections | 19789 | |
Completeness [%] | 81.3 | 42.4 |
Redundancy | 2.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, sitting drop * | 8 | PROTEIN: 12 MG/ML IN 50 MM TRIS/HCL, PH 8.0, MIXED 5:1 WITH 40% (W/V) PEG 1000; RESERVOIR: 0.18-0.20 M SODIUM PHOSPHATE, PH 8.0 HARVESTED IN: 3 M SODIUM ACETATE, PH 7.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 12 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 50 (mM) | |
3 | 1 | reservoir | PEG | 40 (%(w/v)) | |
4 | 1 | reservoir | sodium potassium phosphate | 0.18-0.20 (M) |