8VVO
Structure of FabS1CE2-EPR1-1 in complex with the erythropoietin receptor
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-E |
Synchrotron site | APS |
Beamline | 24-ID-E |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2023-04-06 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.9792 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 71.246, 90.576, 214.850 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 83.460 - 3.090 |
R-factor | 0.2547 |
Rwork | 0.253 |
R-free | 0.28900 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.004 |
RMSD bond angle | 0.857 |
Data reduction software | autoPROC |
Data scaling software | Aimless |
Phasing software | PHENIX |
Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 107.430 | 3.310 |
High resolution limit [Å] | 3.090 | 3.090 |
Rmerge | 0.358 | 1.807 |
Rmeas | 0.390 | 1.953 |
Rpim | 0.152 | 0.734 |
Number of reflections | 25960 | 4627 |
<I/σ(I)> | 5.3 | 1 |
Completeness [%] | 99.2 | 99.7 |
Redundancy | 6.5 | 6.9 |
CC(1/2) | 0.987 | 0.487 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6 | 298 | 0.1 M MMT buffer pH 6.0, 25% PEG1500 |