8C3J
Stapled peptide SP2 in complex with humanised RadA mutant HumRadA22
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I03 |
| Synchrotron site | Diamond |
| Beamline | I03 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-07-27 |
| Detector | DECTRIS EIGER2 XE 16M |
| Wavelength(s) | 0.9795 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 112.560, 112.560, 140.785 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 87.920 - 3.020 |
| R-factor | 0.2503 |
| Rwork | 0.249 |
| R-free | 0.28060 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6hqu |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.389 |
| Data reduction software | autoPROC |
| Data scaling software | autoPROC |
| Phasing software | PHASER |
| Refinement software | BUSTER (1.19.2_4158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 87.920 | 3.070 |
| High resolution limit [Å] | 3.020 | 3.020 |
| Rmeas | 0.242 | |
| Number of reflections | 18416 | 13512 |
| <I/σ(I)> | 10 | 0.9 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 12.8 | 13.8 |
| CC(1/2) | 1.000 | 0.300 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | Protein in 20 mM CHES pH 9.5, 100 mM NaCl. Condition: 8 % w/v PEG 8000 (precipitant) 0.08 M Potassium phosphate pH 5.6 (buffer) 200:200 uL drop |
