1YJM
Crystal structure of the FHA domain of mouse polynucleotide kinase in complex with an XRCC4-derived phosphopeptide.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.3.1 |
| Synchrotron site | ALS |
| Beamline | 8.3.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-06-17 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.1159 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 51.155, 122.999, 136.710 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.200 |
| R-factor | 0.21253 |
| Rwork | 0.211 |
| R-free | 0.24278 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | The FHA domain from the full-length mouse PNK structure 1yj5 |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.862 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.240 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Number of reflections | 18994 | |
| <I/σ(I)> | 8.8 | 3.4 |
| Completeness [%] | 89.4 | 70.2 |
| Redundancy | 2.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 293 | 0.1M Na citrate (pH 5.5), 25% PEG 4000, 0.2M Li2SO4, 5mM DTT, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
