2PDU
Human aldose reductase mutant C303D complexed with IDD393.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU300 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2006-03-05 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 |
Unit cell lengths | 40.130, 47.250, 47.340 |
Unit cell angles | 76.27, 67.37, 77.06 |
Refinement procedure
Resolution | 30.000 - 1.550 |
R-factor | 0.159 |
Rwork | 0.157 |
R-free | 0.21200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1el3 |
RMSD bond length | 0.009 |
RMSD bond angle | 2.200 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | CNS |
Refinement software | SHELXL-97 |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.580 |
High resolution limit [Å] | 1.550 | 1.550 |
Rmerge | 0.029 | 0.126 |
Number of reflections | 38314 | |
<I/σ(I)> | 29 | 6.2 |
Completeness [%] | 85.2 | 68.3 |
Redundancy | 1.8 | 1.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 | 293 | 20 % PEG 6000 in 120 mM ammonium citrate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |