3U3Z
Structure of human microcephalin (MCPH1) tandem BRCT domains in complex with an H2A.X peptide phosphorylated at Ser139 and Tyr142
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X29A |
| Synchrotron site | NSLS |
| Beamline | X29A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-02-25 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9795 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 37.689, 46.537, 55.778 |
| Unit cell angles | 90.00, 97.07, 90.00 |
Refinement procedure
| Resolution | 23.790 - 1.500 |
| R-factor | 0.129 |
| Rwork | 0.129 |
| R-free | 0.17100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3szm |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.071 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE: 1.6.1_357)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.550 |
| High resolution limit [Å] | 1.500 | 1.500 |
| Rmerge | 0.062 | 0.437 |
| Number of reflections | 29928 | |
| <I/σ(I)> | 25.7 | 2.3 |
| Completeness [%] | 96.7 | 80.1 |
| Redundancy | 3 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.6 | 295 | 22% PEG3350, 0.03 M citric acid, 0.07 M Bis-Tris-propane, pH 7.6, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
