8BBS
Structure of AKR1C3 in complex with a bile acid fused tetrazole inhibitor
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | BESSY BEAMLINE 14.1 |
Synchrotron site | BESSY |
Beamline | 14.1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2019-09-26 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.9184 |
Spacegroup name | P 1 |
Unit cell lengths | 39.462, 51.413, 77.879 |
Unit cell angles | 77.26, 86.74, 77.63 |
Refinement procedure
Resolution | 45.930 - 1.400 |
R-factor | 0.155 |
Rwork | 0.155 |
R-free | 0.17750 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1zq5 |
RMSD bond length | 0.011 |
RMSD bond angle | 1.743 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0232) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 45.930 | 45.930 | 1.480 |
High resolution limit [Å] | 1.400 | 4.180 | 1.400 |
Rmerge | 0.058 | 0.029 | 0.582 |
Rmeas | 0.068 | 0.034 | 0.679 |
Total number of observations | 383345 | ||
Number of reflections | 107028 | 4050 | 17252 |
<I/σ(I)> | 12.49 | 37.65 | 2.13 |
Completeness [%] | 93.1 | 93.9 | 92.7 |
Redundancy | 3.582 | 3.548 | 3.638 |
CC(1/2) | 0.999 | 0.998 | 0.828 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 295 | 12.5% w/v PEG 1000, 12.5% w/v PEG 3350, 12.5% v/v MPD and 0.02 M each of DL-glutamic acid monohydrate, DL-alanine, glycine, DL-lysine monohydrochloride, and DL-serine; in 0.1 M bicine/Trizma base, pH 8.5 |