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 |