1EF3
FIDARESTAT BOUND TO HUMAN ALDOSE REDUCTASE
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | MACSCIENCE |
Temperature [K] | 281 |
Detector technology | IMAGE PLATE |
Collection date | 1998-07-06 |
Detector | MAC Science DIP-2000 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 96.140, 62.560, 118.990 |
Unit cell angles | 90.00, 101.60, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.800 |
R-factor | 0.191 |
Rwork | 0.186 |
R-free | 0.27800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ads |
RMSD bond length | 0.014 |
RMSD bond angle | 23.200 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 999.000 | 2.850 |
High resolution limit [Å] | 2.800 | 2.800 |
Rmerge | 0.070 | |
Total number of observations | 27091 * | |
Number of reflections | 15960 | |
Completeness [%] | 92.4 | 81.7 |
Redundancy | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 277 | 1.8M ammonium sulfate, 2% PEG400, 0.1 M HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | ammonium sulfate | 1.8 (M) | |
2 | 1 | reservoir | PEG400 | 2 (%) | |
3 | 1 | reservoir | HEPES/NaOH | 0.1 (M) |