1PIF
PIG ALPHA-AMYLASE
Experimental procedure
Source type | ROTATING ANODE |
Source details | RIGAKU RUH2R |
Temperature [K] | 275 |
Detector technology | IMAGE PLATE |
Collection date | 1995-07-14 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 70.700, 114.900, 118.900 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 7.000 - 2.300 |
R-factor | 0.171 |
Rwork | 0.171 |
R-free | 0.20800 |
Structure solution method | PATTERSON SEARCH |
Starting model (for MR) | PIG PANCREAS ALPHA-AMYLASE (REFERENCE 1) |
RMSD bond length | 0.008 |
RMSD bond angle | 25.400 * |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((AGROVATA) |
Phasing software | X-PLOR (3.1) |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 22.300 | 2.400 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.082 | |
Number of reflections | 41481 | |
Completeness [%] | 95.2 | 81.5 |
Redundancy | 3.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 6 | pH 6.0 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 25 (mg/ml) | |
2 | 1 | drop | cacodylate | 0.01 (M) | |
3 | 1 | drop | 0.02 (M) |