1UH4
Thermoactinomyces vulgaris R-47 alpha-amylase 1/malto-tridecaose 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 | 120.880, 50.519, 108.073 |
Unit cell angles | 90.00, 103.43, 90.00 |
Refinement procedure
Resolution | 31.000 - 1.800 |
R-factor | 0.165 |
Rwork | 0.165 |
R-free | 0.20000 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.006 |
RMSD bond angle | 24.600 * |
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] | 31.000 | 1.890 |
High resolution limit [Å] | 1.800 | 1.800 |
Rmerge | 0.065 | 0.183 |
Total number of observations | 434509 * | |
Number of reflections | 58990 | |
<I/σ(I)> | 5.9 | 3.7 |
Completeness [%] | 99.7 | 98.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | other * | 6.5 | 293 | Kondo, S., (2000) Protein Pept.Letters, 7, 197. * |