8VU1
Structure of FabS1CE3-EPR-1, an elbow-locked high affinity antibody for the erythropoeitin receptor (trigonal form)
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) | 0.97918 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 73.608, 73.608, 153.886 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 63.750 - 3.080 |
| R-factor | 0.2375 |
| Rwork | 0.235 |
| R-free | 0.27670 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.633 |
| Data reduction software | autoPROC |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 153.890 | 3.110 |
| High resolution limit [Å] | 2.930 | 2.930 |
| Rmerge | 0.075 | 2.384 |
| Rmeas | 0.079 | 2.507 |
| Rpim | 0.025 | 0.767 |
| Number of reflections | 10941 | 1727 |
| <I/σ(I)> | 19.9 | 1 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 10 | 10.6 |
| CC(1/2) | 1.000 | 0.496 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 9 | 298 | 0.1 M PCPT buffer pH 9.0, 25% PEG1500 |






