1UH2
Thermoactinomyces vulgaris R-47 alpha-amylase/malto-hexaose complex
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44XU |
| Synchrotron site | SPring-8 |
| Beamline | BL44XU |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2003-03-10 |
| Detector | MACSCIENCE |
| Wavelength(s) | 1.0 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 121.630, 50.491, 108.015 |
| Unit cell angles | 90.00, 103.82, 90.00 |
Refinement procedure
| Resolution | 27.000 - 2.000 |
| R-factor | 0.184 |
| Rwork | 0.184 |
| R-free | 0.21700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 24.500 * |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | CNS (1.1) |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 27.000 | 2.100 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.085 | 0.168 |
| Total number of observations | 513671 * | |
| Number of reflections | 43343 | |
| <I/σ(I)> | 4.5 | 3.8 |
| Completeness [%] | 99.9 | 99.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | other * | 6.5 | 293 | Kondo, S., (2000) Protein Pept.Letters, 7, 197. * |
