4QX4
Human Aldose Reductase complexed with a ligand with a new scaffold at 1.26 A
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 | CCD |
Collection date | 2013-12-13 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.91841 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 49.430, 66.932, 47.411 |
Unit cell angles | 90.00, 91.92, 90.00 |
Refinement procedure
Resolution | 17.841 - 1.259 |
R-factor | 0.1335 |
Rwork | 0.133 |
R-free | 0.15310 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2dux |
RMSD bond length | 0.006 |
RMSD bond angle | 1.218 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.8.4_1496)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.280 |
High resolution limit [Å] | 1.260 | 1.260 |
Number of reflections | 79172 | |
<I/σ(I)> | 21.6 | 3.9 |
Completeness [%] | 95.0 | 90.4 |
Redundancy | 2.7 | 2.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 291 | 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. The well solution for crystallization was 120mM di-Ammonium hydrogen citrate with 20% PEG6000, VAPOR DIFFUSION, HANGING DROP, temperature 291K |