3W0U
human Glyoxalase I with an N-hydroxypyridone inhibitor
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 HF |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2009-08-11 |
| Detector | RIGAKU RAXIS VII |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 86.170, 67.380, 68.480 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 31.820 - 1.700 |
| R-factor | 0.2159 |
| Rwork | 0.214 |
| R-free | 0.24230 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3vw9 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.234 |
| Data reduction software | XDS |
| Data scaling software | SCALA (3.3.12) |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 31.820 | 31.820 | 1.740 |
| High resolution limit [Å] | 1.695 | 7.580 | 1.700 |
| Rmerge | 0.026 | 0.560 | |
| Rmeas | 0.028 | 0.612 | |
| Rpim | 0.011 | 0.245 | |
| Total number of observations | 3508 | 19759 | |
| Number of reflections | 44934 | ||
| <I/σ(I)> | 19.1 | 39.1 | 3.4 |
| Completeness [%] | 99.9 | 98.4 | 99.7 |
| Redundancy | 6.8 | 6.1 | 6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 25% (w/v) PEG 2000 MME, 10%(v/v) Glycerol, 0.1M Na-HEPES (pH 7.0), vapor diffusion, hanging drop, temperature 293K |
