8B34
Structure of Human Aldose Reductase Mutant A299G with a Citrate Molecule Bound in the Anion Binding Pocket
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.2 |
| Synchrotron site | BESSY |
| Beamline | 14.2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2020-02-01 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.918400 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 47.374, 66.845, 49.333 |
| Unit cell angles | 90.00, 91.90, 90.00 |
Refinement procedure
| Resolution | 47.350 - 0.970 |
| R-factor | 0.1059 |
| Rwork | 0.106 |
| R-free | 0.11400 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4prr |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.072 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.18.2_3874) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.350 | 1.030 |
| High resolution limit [Å] | 0.970 | 0.970 |
| Number of reflections | 172687 | 26106 |
| <I/σ(I)> | 18 | 5.8 |
| Completeness [%] | 95.2 | 89.2 |
| Redundancy | 4.1 | 3.8 |
| CC(1/2) | 0.998 | 0.970 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5 | 291 | 50 mM Di-Ammoniumhydrogen citrate pH 5: 15 mg/mL hAR, 5.2 mg/mL DTT, 0.7 mg/mL NADP+, 5% (w/v) PEG 6000; Reservoir: 120 mM Di-Ammoniumhydrogen citrate pH 5, 20% (w/v) PEG 6000 |
