8VTR
Structure of FabS1CE3-EPR-1, an elbow-locked high affinity antibody for the erythropoeitin receptor (orthorhombic 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 21 21 21 |
| Unit cell lengths | 73.199, 74.275, 93.335 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 58.120 - 1.960 |
| R-factor | 0.1893 |
| Rwork | 0.187 |
| R-free | 0.22750 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.976 |
| 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] | 74.280 | 2.010 |
| High resolution limit [Å] | 1.960 | 1.960 |
| Rmerge | 0.073 | 0.686 |
| Rmeas | 0.079 | |
| Rpim | 0.031 | 0.302 |
| Number of reflections | 37275 | 2602 |
| <I/σ(I)> | 18.5 | 2.3 |
| Completeness [%] | 99.9 | 99.7 |
| Redundancy | 6.5 | 6 |
| CC(1/2) | 0.999 | 0.855 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 298 | 0.2 M Ammonium Citrate dibasic, 20% PEG3350. This was set up as a Fab/EPOR complex, however no EPOR was observed upon solving the structure. |
