2X0U
STRUCTURE OF THE P53 CORE DOMAIN MUTANT Y220C BOUND TO A 2-amino substituted benzothiazole scaffold
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I02 |
Synchrotron site | Diamond |
Beamline | I02 |
Temperature [K] | 100 |
Detector technology | CCD |
Detector | ADSC CCD |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 65.060, 71.140, 105.410 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 24.712 - 1.600 |
R-factor | 0.1663 |
Rwork | 0.165 |
R-free | 0.19330 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2j1x |
RMSD bond length | 0.007 |
RMSD bond angle | 1.120 |
Phasing software | PHENIX |
Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 35.500 | 1.690 |
High resolution limit [Å] | 1.600 | 1.600 |
Rmerge | 0.070 | 0.310 |
Number of reflections | 65261 | |
<I/σ(I)> | 15.8 | 5.2 |
Completeness [%] | 99.9 | 100 |
Redundancy | 6.2 | 5.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.2 | 294 | SITTING DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES PH 7.2, 19% PEG 4000, 5 MM DTT. SOAKING BUFFER: SATURATED SOLUTION OF SMALL MOLECULE LIGAND IN 100 MM HEPES PH 7.2, 10 MM SODIUM PHOSPHATE PH 7.2, 19% PEG 4000, 20% GLYCEROL, 150 MM KCL. |