1EKO
PIG ALDOSE REDUCTASE COMPLEXED WITH IDD384 INHIBITOR
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | LURE BEAMLINE DW32 |
| Synchrotron site | LURE |
| Beamline | DW32 |
| Temperature [K] | 273 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-03-08 |
| Detector | MARRESEARCH |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 68.810, 68.810, 154.770 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 2.200 |
| R-factor | 0.179 * |
| Rwork | 0.216 |
| R-free | 0.27300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | ALDOSE REDUCTASE NATIVE |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.400 |
| Data reduction software | XDS |
| Phasing software | X-PLOR |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 2.300 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.086 | 0.245 |
| Number of reflections | 19184 | |
| <I/σ(I)> | 22.5 | 3.1 |
| Completeness [%] | 98.1 | 97.5 |
| Redundancy | 5 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.2 | 277 | Rogniaux, H., (1999) J. Am. Soc. Mass Spectrom., 10, 635. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 15 (mg/ml) | |
| 3 | 1 | drop | NADP+ | ||
| 4 | 1 | drop | MES | 75 (mM) | |
| 5 | 1 | drop | EDTA | 1 (mM) | |
| 6 | 1 | drop | dithiothreitol | 1 (mM) | |
| 7 | 1 | drop | PEG6000 | 2.5 (%(w/v)) | |
| 8 | 1 | reservoir | PEG6000 | 25 (%) |
