7EXE
Crystal structure of mouse 14-3-3zeta in complex with doubly phosphorylated ADAM22 peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL45XU |
Synchrotron site | SPring-8 |
Beamline | BL45XU |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2015-05-12 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 1.0 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 72.197, 85.546, 111.869 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 49.480 - 2.750 |
R-factor | 0.2436 |
Rwork | 0.242 |
R-free | 0.26660 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1qja |
RMSD bond length | 0.003 |
RMSD bond angle | 0.412 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | MOLREP |
Refinement software | PHENIX (1.17.1_3660) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 49.500 | 2.920 |
High resolution limit [Å] | 2.750 | 2.750 |
Rmeas | 0.351 | 2.311 |
Number of reflections | 18575 | 2927 |
<I/σ(I)> | 14.13 | 1.38 |
Completeness [%] | 99.9 | 99.8 |
Redundancy | 12.9 | 13.5 |
CC(1/2) | 0.998 | 0.918 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | PEG2000MME |