8RB6
Structure of Aldo-Keto Reductase 1C3 (AKR1C3) in complex with an inhibitor M689, with the 3-hydroxy-benzoisoxazole moiety. Resolution 2.0A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MAX IV BEAMLINE BioMAX |
Synchrotron site | MAX IV |
Beamline | BioMAX |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2022-09-22 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.9762 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 41.343, 93.191, 83.008 |
Unit cell angles | 90.00, 95.09, 90.00 |
Refinement procedure
Resolution | 61.850 - 2.000 |
R-factor | 0.1917 |
Rwork | 0.190 |
R-free | 0.22660 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6f2u |
RMSD bond length | 0.003 |
RMSD bond angle | 0.603 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX ((1.19.2_4158: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 61.850 | 2.050 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.100 | 0.602 |
Rmeas | 0.108 | 0.652 |
Rpim | 0.041 | 0.247 |
Total number of observations | 296998 | 21558 |
Number of reflections | 42384 | 3131 |
<I/σ(I)> | 9 | 3 |
Completeness [%] | 100.0 | |
Redundancy | 7 | 6.9 |
CC(1/2) | 0.997 | 0.944 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 279 | 0.1 M MESH, 25% PEG3350 |