6T27
Structure of Human Aldose Reductase Mutant L301A with a Citrate Molecule Bound in the Anion Binding Pocket
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.1 |
| Synchrotron site | BESSY |
| Beamline | 14.1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-08-11 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.9184 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 47.266, 66.625, 49.345 |
| Unit cell angles | 90.00, 92.07, 90.00 |
Refinement procedure
| Resolution | 47.240 - 1.110 |
| R-factor | 0.1045 |
| Rwork | 0.104 |
| R-free | 0.12130 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4prr |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.004 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.16_3549) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.240 | 1.180 |
| High resolution limit [Å] | 1.110 | 1.110 |
| Number of reflections | 111606 | 17437 |
| <I/σ(I)> | 17.76 | 6.79 |
| Completeness [%] | 92.3 | 89.3 |
| Redundancy | 3.9 | 3.9 |
| CC(1/2) | 0.998 | 0.972 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING 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 |
