1BLI
BACILLUS LICHENIFORMIS ALPHA-AMYLASE
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH2R |
| Temperature [K] | 278 |
| Detector technology | IMAGE PLATE |
| Collection date | 1997-05 |
| Detector | MARRESEARCH |
| Spacegroup name | P 61 |
| Unit cell lengths | 91.300, 91.300, 137.700 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.000 - 1.900 |
| R-factor | 0.154 |
| Rwork | 0.154 |
| R-free | 0.18500 |
| Structure solution method | PATTERSON SEARCH |
| Starting model (for MR) | 1bpl |
| RMSD bond length | 0.013 |
| RMSD bond angle | 25.700 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 27.500 | 1.930 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.084 | 0.418 |
| Number of reflections | 46801 | |
| <I/σ(I)> | 23 | 2.3 |
| Completeness [%] | 91.5 | 82.9 |
| Redundancy | 6.7 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 7 | 20 * | drop consists of equal volume of protein and reservoir solutions * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 50 (mM) | |
| 3 | 1 | reservoir | HEPES | 50 (mM) | |
| 4 | 1 | reservoir | PEG500 | 1 (%(v/v)) |
