6FNB
Mono- and bivalent 14-3-3 inhibitors for characterizing supramolecular lysine-PEG interactions in proteins
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X10SA |
Synchrotron site | SLS |
Beamline | X10SA |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-09-20 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 1.000 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 71.800, 103.310, 113.060 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 46.980 - 2.300 |
R-factor | 0.216 |
Rwork | 0.214 |
R-free | 0.24840 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3nkx |
RMSD bond length | 0.007 |
RMSD bond angle | 1.072 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER (2.3.0) |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 46.980 | 46.980 | 2.400 |
High resolution limit [Å] | 2.300 | 40.000 | 2.300 |
Rmerge | 0.128 | 0.082 | 1.106 |
Rmeas | 0.134 | 0.086 | 1.151 |
Total number of observations | 505296 | ||
Number of reflections | 38130 | 4 | 4494 |
<I/σ(I)> | 12.09 | 24 | 2.42 |
Completeness [%] | 100.0 | 28.6 | 99.9 |
Redundancy | 13.252 | 9.75 | 13.04 |
CC(1/2) | 0.996 | 0.996 | 0.858 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 277.15 | 0.09 M HEPES sodium salt pH 7.5 1.26 M tri-Sodium citrate 10 %(v/v) Glycerol |