4YU1
Human Aldose Reductase complexed with Schl12134 (3-[5-(3-nitrophenyl)-2-thienyl]propanoic acid) at 1.02 A
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 | 2015-02-07 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.91841 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 49.449, 66.354, 47.429 |
| Unit cell angles | 90.00, 92.31, 90.00 |
Refinement procedure
| Resolution | 24.704 - 1.020 |
| R-factor | 0.1335 |
| Rwork | 0.133 |
| R-free | 0.14970 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2dux |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.371 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.8.4_1492)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.080 |
| High resolution limit [Å] | 1.020 | 1.020 |
| Number of reflections | 150587 | |
| <I/σ(I)> | 14.02 | 2.48 |
| Completeness [%] | 96.7 | 92.9 |
| Redundancy | 3.4 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5 | 291 | Crystallization solution: 50 mM di-Ammoniumhydrogen citrate pH 5.0 PEG6000= 5 % (m/V) DTT= 5.15 g/L NADP+= 0.66 g/L and Human Aldose Reductase= 15 mg/ml.Afterwards the crystals were soaked into Tris 100 mM 25% (m/V) PEG6000 pH 8.0 saturated with the inhibitor. |
