8QWK
Structure of p53 cancer mutant Y126C
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06SA |
Synchrotron site | SLS |
Beamline | X06SA |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2019-07-05 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.9999 |
Spacegroup name | P 65 2 2 |
Unit cell lengths | 45.188, 45.188, 331.301 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 39.100 - 1.690 |
R-factor | 0.196997491503 |
Rwork | 0.196 |
R-free | 0.21808 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.006 |
RMSD bond angle | 0.799 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 39.100 | 1.720 |
High resolution limit [Å] | 1.690 | 1.690 |
Rmerge | 0.053 | 0.932 |
Number of reflections | 24105 | 1190 |
<I/σ(I)> | 17.6 | 2.4 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 7.2 | 7.7 |
CC(1/2) | 0.999 | 0.803 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | Protein solution: 5.5-6.0 mg/ml in 25 mM HEPES (pH 7.5), 300 mM NaCl, 0.5 mM TCEP. Reservoir buffer: 0.7 M sodium citrate and 0.1 M bis-tris-propane (pH 7.0). |