1HNY
The structure of human pancreatic alpha-amylase at 1.8 angstroms resolution and comparisons with related enzymes
Experimental procedure
| Detector technology | IMAGE PLATE |
| Detector | RIGAKU |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 53.040, 74.800, 137.340 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 1.800 |
| R-factor | 0.174 |
| Rwork | 0.174 |
| RMSD bond length | 0.016 |
| RMSD bond angle | 0.036 * |
| Data reduction software | MSC |
| Phasing software | X-PLOR (2.1) |
| Refinement software | PROLSQ |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 36.600 | |
| High resolution limit [Å] | 1.800 | 1.800 * |
| Rmerge | 0.055 | |
| Number of reflections | 42316 | |
| Completeness [%] | 82.1 | 63.1 * |
| Redundancy | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 * | 22 * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 20 (mg/ml) | |
| 2 | 1 | drop | 1 (mM) | ||
| 3 | 1 | drop | cacodylate | 100 (mM) | |
| 4 | 1 | reservoir | MPD | 60 (%) |






