5W7X
Crystal Structure of FHA domain of human APLF in complex with XRCC1 bisphospho peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-11-22 |
Detector | RIGAKU SATURN 944+ |
Wavelength(s) | 1.514 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 59.119, 36.799, 98.284 |
Unit cell angles | 90.00, 90.86, 90.00 |
Refinement procedure
Resolution | 25.497 - 2.005 |
R-factor | 0.194 |
Rwork | 0.192 |
R-free | 0.22910 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5w7w |
RMSD bond length | 0.003 |
RMSD bond angle | 0.581 |
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] | 25.497 | 2.050 |
High resolution limit [Å] | 2.005 | 2.005 |
Rpim | 0.031 | 0.214 |
Number of reflections | 28032 | 1098 |
<I/σ(I)> | 13.4 | |
Completeness [%] | 97.9 | 75.3 |
Redundancy | 4.8 | 2.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 0.6mM XRCC1 bisphosphopeptide 0.6mM APLF 0.5M lithium chloride 0.1M Tris 28% PEG 6000 |