8FH5
Crystal Structure Of Aldose Reductase (AKR1B1) Complexed With NADP+ And AT-001
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL12-2 |
Synchrotron site | SSRL |
Beamline | BL12-2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2019-04-03 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.97946 |
Spacegroup name | P 1 |
Unit cell lengths | 40.144, 47.026, 47.340 |
Unit cell angles | 75.87, 67.43, 76.78 |
Refinement procedure
Resolution | 36.674 - 1.620 |
Rwork | 0.143 |
R-free | 0.16720 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.011 |
RMSD bond angle | 1.769 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0403) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 36.674 | 1.650 |
High resolution limit [Å] | 1.620 | 1.620 |
Rmerge | 0.042 | 0.145 |
Rmeas | 0.059 | 0.205 |
Rpim | 0.042 | 0.145 |
Number of reflections | 34509 | 1727 |
<I/σ(I)> | 16.7 | |
Completeness [%] | 88.6 | |
Redundancy | 3.8 | 3.9 |
CC(1/2) | 0.998 | 0.976 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 298 | 25% PEG 3350, 100 mM Bis-Tris |