7P3I
Crystal structure of human CD40/TNFRSF5 in complex with the anti-CD40 DARPin protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2020-07-08 |
| Detector | DECTRIS EIGER2 X 16M |
| Wavelength(s) | 0.999812 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 193.670, 59.564, 81.842 |
| Unit cell angles | 90.00, 106.99, 90.00 |
Refinement procedure
| Resolution | 92.610 - 2.290 |
| R-factor | 0.2216 |
| Rwork | 0.220 |
| R-free | 0.25250 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | none |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.587 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0155) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 92.610 | 2.326 |
| High resolution limit [Å] | 2.286 | 2.286 |
| Rmerge | 0.078 | 1.149 |
| Number of reflections | 39800 | 8538 |
| <I/σ(I)> | 10.1 | 1.3 |
| Completeness [%] | 97.8 | 97.3 |
| Redundancy | 4.3 | 4.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 277 | 29.9999 %w/v PEG 4K, 0.24 M LiSO4, 0.0999 M TRIS, 0.35 M NaBr |
