5YQG
The structure of 14-3-3 and pNumb peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL17U1 |
Synchrotron site | SSRF |
Beamline | BL17U1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-10-20 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.987 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 59.260, 74.626, 134.136 |
Unit cell angles | 90.00, 90.07, 90.00 |
Refinement procedure
Resolution | 49.883 - 2.100 |
R-factor | 0.1858 |
Rwork | 0.184 |
R-free | 0.22370 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4hkc |
RMSD bond length | 0.007 |
RMSD bond angle | 0.803 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | PHENIX ((1.10.1_2155: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.140 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.086 | |
Number of reflections | 66596 | |
<I/σ(I)> | 2.1 | |
Completeness [%] | 98.2 | |
Redundancy | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 290.15 | tri-Sodium Citrate dihydrate, isopropanol, PEG 4000 |