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. * |