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 |
