8T5F
De novo design of high-affinity protein binders to bioactive helical peptides
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-C |
| Synchrotron site | APS |
| Beamline | 24-ID-C |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2023-04-05 |
| Detector | DECTRIS EIGER2 X 16M |
| Wavelength(s) | 0.97911 |
| Spacegroup name | P 4 21 2 |
| Unit cell lengths | 91.324, 91.324, 37.732 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.840 - 1.990 |
| R-factor | 0.2206 |
| Rwork | 0.219 |
| R-free | 0.25080 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.043 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX (dev_4761) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.840 | 2.040 |
| High resolution limit [Å] | 1.990 | 1.990 |
| Rmerge | 0.120 | |
| Number of reflections | 11302 | 738 |
| <I/σ(I)> | 21.8 | 1.3 |
| Completeness [%] | 98.6 | 94.6 |
| Redundancy | 15.1 | 15.2 |
| CC(1/2) | 0.999 | 0.545 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.5 | 293 | 0.2 M Sodium chloride, 0.1 M Sodium acetate pH 4.5, and 1.26 M Ammonium sulfate |
