1AQH
ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH2R |
| Temperature [K] | 288 |
| Detector technology | IMAGE PLATE |
| Collection date | 1996-12 |
| Detector | MARRESEARCH |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 71.400, 138.700, 115.700 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 43.000 - 2.000 |
| R-factor | 0.157 |
| Rwork | 0.157 |
| R-free | 0.20400 |
| Structure solution method | PHASES FROM ALPHA-AMYLASE COMPLEXED WITH A TRIS MOLECULE COMBINED WITH STRUCTURE FACTORS FROM THIS NATIVE DATA SET |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.184 * |
| Data reduction software | DENZO |
| Data scaling software | Agrovata |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR (3.843) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 43.000 | 2.110 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.142 * | 0.142 * |
| Total number of observations | 93724 * | |
| Number of reflections | 31485 | |
| <I/σ(I)> | 5 | 1.1 |
| Completeness [%] | 80.5 | 31.5 |
| Redundancy | 3 | 1.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7 | Aghajari, N., (1996) Protein Sci., 5, 2128. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | MPD | 60-70 (%) | |
| 2 | 1 | reservoir | HEPES | 0.1 (M) |






