1IZJ
Thermoactinomyces vulgaris R-47 alpha-amylase 1 mutant enzyme f313a
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU300 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2001-11-29 |
| Detector | RIGAKU RAXIS IIC |
| Wavelength(s) | 1.0 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 120.944, 50.417, 107.920 |
| Unit cell angles | 90.00, 103.56, 90.00 |
Refinement procedure
| Resolution | 25.000 * - 2.200 |
| R-factor | 0.18 |
| Rwork | 0.179 |
| R-free | 0.22000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 24.700 * |
| Data scaling software | SCALA |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 58.790 |
| High resolution limit [Å] | 2.200 |
| Rmerge | 0.069 |
| Total number of observations | 162092 * |
| Number of reflections | 31175 * |
| Completeness [%] | 100.0 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 293 | Kondo, S., (2000) Protein Pept. Letters, 7, 197. * |
