1IZK
Thermoactinomyces vulgaris R-47 alpha-amylase 1 mutant enzyme w398v
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | PHOTON FACTORY BEAMLINE BL-18B |
| Synchrotron site | Photon Factory |
| Beamline | BL-18B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-07-07 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.5418 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 122.720, 50.820, 108.820 |
| Unit cell angles | 90.00, 104.19, 90.00 |
Refinement procedure
| Resolution | 25.000 * - 2.200 |
| R-factor | 0.196 |
| Rwork | 0.192 |
| R-free | 0.23700 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 * |
| RMSD bond angle | 24.600 * |
| Data scaling software | SCALEPACK |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 25.410 |
| High resolution limit [Å] | 2.200 |
| Rmerge | 0.072 |
| Total number of observations | 412389 * |
| Number of reflections | 33199 * |
| 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. * |
