9FFD
STRUCTURE OF ALDO-KETO REDUCTASE 1C3 (AKR1C3) IN COMPLEX WITH AN INHIBITOR MEDS765
This is a non-PDB format compatible entry.
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 | 2024-02-16 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1.0000 |
Spacegroup name | P 1 |
Unit cell lengths | 46.228, 48.791, 83.314 |
Unit cell angles | 74.12, 85.35, 69.60 |
Refinement procedure
Resolution | 34.510 - 1.750 |
R-factor | 0.1626 |
Rwork | 0.161 |
R-free | 0.19650 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.005 |
RMSD bond angle | 0.858 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX ((1.21.1_5286: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.820 | 1.780 |
High resolution limit [Å] | 1.750 | 1.750 |
Rmerge | 0.043 | 0.280 |
Rmeas | 0.051 | 0.334 |
Rpim | 0.027 | 0.178 |
Total number of observations | 233261 | 10987 |
Number of reflections | 64261 | 3222 |
<I/σ(I)> | 12.4 | 3.4 |
Completeness [%] | 97.0 | |
Redundancy | 3.6 | 3.4 |
CC(1/2) | 0.996 | 0.957 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6 | 279 | 0.1 M MES, 24% PEG3350, PH 6.0 |