1Y98
Structure of the BRCT repeats of BRCA1 bound to a CtIP phosphopeptide.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X12B |
Synchrotron site | NSLS |
Beamline | X12B |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-11-10 |
Detector | ADSC QUANTUM 4 |
Wavelength(s) | 1.0000 |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 113.118, 113.118, 121.876 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 19.590 - 2.500 |
R-factor | 0.236 |
Rwork | 0.234 |
R-free | 0.26960 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1t15 |
RMSD bond length | 0.016 |
RMSD bond angle | 1.781 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Number of reflections | 16294 | |
<I/σ(I)> | 17.53 | 2.68 |
Completeness [%] | 99.1 | 99.4 |
Redundancy | 11 | 6.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | AMMONIUM SULPHATE, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |