1GZH
Crystal structure of the BRCT domains of human 53BP1 bound to the p53 tumor supressor
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2000-05-15 |
Detector | MAR scanner 345 mm plate |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 71.520, 94.570, 136.200 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 500.000 * - 2.600 |
R-factor | 0.238 |
Rwork | 0.238 |
R-free | 0.28830 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1tsr |
RMSD bond length | 0.008 |
RMSD bond angle | 1.349 * |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 55.000 * | 2.740 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.104 | 0.358 |
Number of reflections | 54119 | |
<I/σ(I)> | 6.2 | 1.4 |
Completeness [%] | 99.1 | 96.9 |
Redundancy | 7.7 | 3.70 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Batch method * | 7.4 | 50 MM TRIS PH 7.4, 250 MM AMMONIUM SULFATE, 25% POLYETHYLENE GLYCOL 4000 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 15 (mg/ml) | |
2 | 1 | 1 | Tris-HCl | 50 (mM) | pH7.4 |
3 | 1 | 1 | ammonium sulfate | ||
4 | 1 | 1 | PEG4000 | 20-25 (%) |