1T2V
Structural basis of phospho-peptide recognition by the BRCT domain of BRCA1, structure with phosphopeptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.3 |
| Synchrotron site | ALS |
| Beamline | 5.0.3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-01-27 |
| Detector | ADSC QUANTUM 4 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 97.117, 138.357, 198.266 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 3.300 |
| R-factor | 0.261 |
| Rwork | 0.258 |
| R-free | 0.30100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.252 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.420 |
| High resolution limit [Å] | 3.303 | 3.300 |
| Rmerge | 0.125 | 0.500 |
| Number of reflections | 20289 | |
| <I/σ(I)> | 11.1 | 2.7 |
| Completeness [%] | 99.9 | 99.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.6 | 298 | PEG 4000 ammonium acetate, tri-sodium citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 5.60 |
