1T15
Crystal Structure of the Brca1 BRCT Domains in Complex with the Phosphorylated Interacting Region from Bach1 Helicase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2004-01-17 |
Detector | RIGAKU RAXIS II |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 65.837, 65.837, 93.075 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 15.000 - 1.850 |
Rwork | 0.206 |
R-free | 0.22200 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 1.350 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 1.930 |
High resolution limit [Å] | 1.850 | 1.850 |
Number of reflections | 19219 | |
Completeness [%] | 93.9 | 76.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | MICROBATCH | 6.5 | 291 | PEG 8000, Ammonium Sulphate, MES, pH 6.5, Microbatch, temperature 291K |