5W7Y
Crystal Structure of FHA domain of human APLF in complex with XRCC1 monophosphorylated mutated peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 HF |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-12-14 |
| Detector | DECTRIS PILATUS 200K |
| Wavelength(s) | 1.514 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 54.799, 31.072, 118.908 |
| Unit cell angles | 90.00, 97.84, 90.00 |
Refinement procedure
| Resolution | 29.449 - 2.100 |
| R-factor | 0.2043 |
| Rwork | 0.203 |
| R-free | 0.23730 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5w7x |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.673 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.449 | 2.140 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rpim | 0.230 | 0.230 |
| Number of reflections | 11773 | 486 |
| <I/σ(I)> | 7.9 | 2.7 |
| Completeness [%] | 92.3 | 87.7 |
| Redundancy | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 0.6mM APLF 0.6mM XRCC1 peptide 0.1M Tris 30% PEG 1000 |
