1QHP
FIVE-DOMAIN ALPHA-AMYLASE FROM BACILLUS STEAROTHERMOPHILUS, MALTOSE COMPLEX
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Detector | MARRESEARCH |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 89.760, 89.760, 185.710 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 1.700 |
| Rwork | 0.153 |
| R-free | 0.19100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1cdg |
| RMSD bond length | 0.008 |
| RMSD bond angle | 0.022 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.730 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.080 | 0.450 |
| Total number of observations | 460513 * | |
| Number of reflections | 87912 * | |
| <I/σ(I)> | 17.8 | 3.1 |
| Completeness [%] | 95.8 | 92.5 |
| Redundancy | 5.3 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 6 | drop consists of 1:1 mixture of well and protein solutions * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | enzyme | 19 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 10 (mM) | |
| 3 | 1 | drop | 0.2 (M) | ||
| 4 | 1 | drop | 5 (mM) | ||
| 5 | 1 | reservoir | 0.9 (M) | ||
| 6 | 1 | reservoir | PEG1450 | 2.5 (%(w/v)) | |
| 7 | 1 | reservoir | TEA | 50 (mM) | |
| 8 | 1 | reservoir | maltose | 100 (mM) |
