3W0T
Human Glyoxalase I with an N-hydroxypyridone derivative inhibitor
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | PHOTON FACTORY BEAMLINE AR-NE3A |
Synchrotron site | Photon Factory |
Beamline | AR-NE3A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-05-20 |
Detector | ADSC QUANTUM 270 |
Wavelength(s) | 1.000 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 66.570, 81.030, 68.620 |
Unit cell angles | 90.00, 90.13, 90.00 |
Refinement procedure
Resolution | 19.770 - 1.351 |
R-factor | 0.1761 |
Rwork | 0.175 |
R-free | 0.19680 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3vw9 |
RMSD bond length | 0.010 |
RMSD bond angle | 1.070 |
Data reduction software | XDS |
Data scaling software | SCALA (3.3.9) |
Phasing software | PHASER (2.1.4) |
Refinement software | BUSTER-TNT (BUSTER 2.11.2) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 23.507 | 23.507 | 1.390 |
High resolution limit [Å] | 1.351 | 6.040 | 1.350 |
Rmerge | 0.033 | 0.725 | |
Rmeas | 0.040 | 0.957 | |
Rpim | 0.021 | 0.615 | |
Total number of observations | 5947 | 15412 | |
Number of reflections | 145439 | ||
<I/σ(I)> | 12.6 | 31.3 | 1.3 |
Completeness [%] | 91.5 | 94 | 56.2 |
Redundancy | 3.5 | 3.4 | 2.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 33% (w/v) PEG 2000 MME, 0.1M Na-HEPES (pH 7.0), vapor diffusion, hanging drop, temperature 293K |