1UH3
Thermoactinomyces vulgaris R-47 alpha-amylase/acarbose complex
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 | 2002-06-10 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 1.0 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 121.611, 50.600, 108.555 |
Unit cell angles | 90.00, 103.77, 90.00 |
Refinement procedure
Resolution | 33.000 - 2.600 |
R-factor | 0.185 |
Rwork | 0.185 |
R-free | 0.25500 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.006 |
RMSD bond angle | 24.800 * |
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] | 33.000 | 2.730 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.087 | 0.167 |
Total number of observations | 276350 * | |
Number of reflections | 20035 | |
<I/σ(I)> | 7.7 | 4.5 |
Completeness [%] | 99.8 | 100 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | other * | 6.5 | 293 | Kondo, S., (2000) Protein Pept.Letters, 7, 197. * |