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 |