7EXQ
Crystal structure of alkaline alpha-galactosidase D383A mutant from Arabidopsis thaliana complexed with product-galactose and sucrose.
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 | 2018-05-03 |
| Detector | RAYONIX MX300HE |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 97.710, 104.101, 182.420 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.880 - 2.200 |
| R-factor | 0.1955 |
| Rwork | 0.193 |
| R-free | 0.25470 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 7exg |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.937 |
| 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 | 2.280 |
| High resolution limit [Å] | 2.200 | 4.730 | 2.200 |
| Rmerge | 0.076 | 0.027 | 0.717 |
| Rmeas | 0.085 | 0.031 | 0.789 |
| Rpim | 0.036 | 0.014 | 0.327 |
| Total number of observations | 500553 | ||
| Number of reflections | 92281 | 9177 | 9381 |
| <I/σ(I)> | 8.9 | ||
| Completeness [%] | 97.2 | 92.4 | 100 |
| Redundancy | 5.4 | 4.7 | 5.6 |
| CC(1/2) | 0.998 | 0.880 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICROBATCH | 291.5 | Tris, PEG2000, PGA |
