8BR9
Stapled peptide SP24 in complex with humanised RadA mutant HumRadA22
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I04 |
| Synchrotron site | Diamond |
| Beamline | I04 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2021-01-19 |
| Detector | DECTRIS EIGER2 X 16M |
| Wavelength(s) | 0.9795 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 140.464, 38.642, 43.528 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 43.530 - 1.630 |
| R-factor | 0.2515 |
| Rwork | 0.250 |
| R-free | 0.28160 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6hqu |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.604 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | BUSTER |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 70.230 | 1.660 |
| High resolution limit [Å] | 1.630 | 1.630 |
| Rmeas | 0.059 | |
| Number of reflections | 30303 | 11733 |
| <I/σ(I)> | 12 | 0.3 |
| Completeness [%] | 98.7 | |
| Redundancy | 7.9 | |
| CC(1/2) | 1.000 | 0.300 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 291.15 | 0.1 M Na 3 Cit 4.2 pH (Buffer) 20 %w/v PEG 1K (Precipitant) 0.2 M Li 2 SO4 (Salt) |
