7EXR
Crystal structure of alkaline alpha-galactosidase D383A mutant from Arabidopsis thaliana complexed with Stachyose.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSRRC BEAMLINE BL15A1 |
Synchrotron site | NSRRC |
Beamline | BL15A1 |
Temperature [K] | 110 |
Detector technology | CCD |
Collection date | 2018-03-28 |
Detector | RAYONIX MX300HE |
Wavelength(s) | 0.97 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 97.589, 103.749, 182.372 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.000 |
R-factor | 0.1692 |
Rwork | 0.167 |
R-free | 0.20640 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 7exg |
RMSD bond length | 0.018 |
RMSD bond angle | 2.010 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 30.000 | 30.000 | 2.070 |
High resolution limit [Å] | 2.000 | 4.310 | 2.000 |
Rmerge | 0.093 | 0.064 | 0.597 |
Rmeas | 0.101 | 0.071 | 0.660 |
Rpim | 0.040 | 0.029 | 0.277 |
Total number of observations | 785125 | ||
Number of reflections | 124558 | 12950 | 12278 |
<I/σ(I)> | 7.2 | ||
Completeness [%] | 99.9 | 99.8 | 99.5 |
Redundancy | 6.3 | 6 | 5.4 |
CC(1/2) | 0.995 | 0.855 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 7.8 | 291.5 | Tris, PEG 2000, PGA |