8GJG
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 | 2022-12-13 |
| Detector | DECTRIS EIGER2 S 16M |
| Wavelength(s) | 0.97918 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 37.793, 45.900, 63.607 |
| Unit cell angles | 90.00, 97.31, 90.00 |
Refinement procedure
| Resolution | 63.090 - 1.950 |
| R-factor | 0.211 |
| Rwork | 0.209 |
| R-free | 0.24910 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.435 |
| 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] | 63.090 | 2.000 |
| High resolution limit [Å] | 1.950 | 1.950 |
| Rmerge | 0.073 | 2.001 |
| Rpim | 0.033 | 0.884 |
| Number of reflections | 15425 | 2387 |
| <I/σ(I)> | 10.1 | 0.6 |
| Completeness [%] | 98.5 | 96.3 |
| Redundancy | 6.7 | 6.8 |
| CC(1/2) | 0.998 | 0.461 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 0.9 M Halogens, 0.1 M Tris- Bicine pH 8.5 Buffer, and 37.5% of 25% v/v MPD; 25% PEG 1000; 25% w/v PEG 3350 mixture |
