1T29
Crystal structure of the BRCA1 BRCT repeats bound to a phosphorylated BACH1 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X25 |
| Synchrotron site | NSLS |
| Beamline | X25 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-01-30 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 1.1 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 63.177, 63.177, 105.532 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 2.300 |
| R-factor | 0.252 |
| Rwork | 0.252 |
| R-free | 0.26600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1jnx |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.690 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 99.000 | 2.400 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.072 | 0.179 |
| Number of reflections | 11209 | |
| <I/σ(I)> | 0.179 | |
| Completeness [%] | 98.9 | 100 |
| Redundancy | 40 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 295 | PEG4000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
