2D2O
Structure of a complex of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with maltohexaose demonstrates the important role of aromatic residues at the reducing end of the substrate binding cleft
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 | 2004-03-03 |
Detector | MACSCIENCE |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 113.690, 118.710, 112.380 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 46.000 - 2.100 |
R-factor | 0.184 |
Rwork | 0.184 |
R-free | 0.21700 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.006 |
RMSD bond angle | 1.300 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 46.370 | 2.370 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.078 | 0.220 |
Number of reflections | 85196 | |
<I/σ(I)> | 12.5 | 4.5 |
Completeness [%] | 95.5 | 97.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.1 | 298 | 1.0 % (w/v) polyethylene glycol 6,000, 2.5mM calcium chloride, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 298K |