3V3B
Structure of the Stapled p53 Peptide Bound to Mdm2
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X10SA |
Synchrotron site | SLS |
Beamline | X10SA |
Temperature [K] | 90 |
Detector technology | PIXEL |
Collection date | 2011-02-07 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 1.0 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 45.400, 42.410, 50.500 |
Unit cell angles | 90.00, 90.86, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.000 |
R-factor | 0.16827 |
Rwork | 0.166 |
R-free | 0.21647 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.009 |
RMSD bond angle | 1.050 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 2.000 |
Number of reflections | 13254 |
Completeness [%] | 99.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4.75 | 290 | 100 mM Na-acetate, 2.5M NaCl, pH 4.75, VAPOR DIFFUSION, SITTING DROP, temperature 290K |