3FDO
Structure of human MDMX in complex with high affinity peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X10SA |
Synchrotron site | SLS |
Beamline | X10SA |
Temperature [K] | 90 |
Detector technology | CCD |
Collection date | 2008-07-15 |
Detector | MARRESEARCH |
Wavelength(s) | 1.0 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 69.230, 30.950, 50.420 |
Unit cell angles | 90.00, 124.41, 90.00 |
Refinement procedure
Resolution | 15.000 - 1.400 |
R-factor | 0.18286 |
Rwork | 0.179 |
R-free | 0.24708 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3dab |
RMSD bond length | 0.008 |
RMSD bond angle | 1.304 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0066) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 1.500 |
High resolution limit [Å] | 1.400 | 1.400 |
Number of reflections | 14843 | |
Completeness [%] | 84.1 | 46.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.3 | 290 | 4.3M NaCl, 100mM Hepes, pH7.3, VAPOR DIFFUSION, SITTING DROP, temperature 290K |