6QBQ
structure of the core domaine of Knr4, an intrinsically disordered protein from Saccharomyces cerevisiae - mutant S200A S203A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-02-03 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 0.97625 |
Spacegroup name | P 62 |
Unit cell lengths | 102.816, 102.816, 92.700 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 45.000 - 2.350 |
R-factor | 0.1963 |
Rwork | 0.195 |
R-free | 0.22398 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5j1b |
RMSD bond length | 0.007 |
RMSD bond angle | 1.010 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0230) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 45.000 | 2.490 |
High resolution limit [Å] | 2.350 | 2.350 |
Rmeas | 0.056 | 1.127 |
Number of reflections | 23243 | 3685 |
<I/σ(I)> | 19.2 | 1.8 |
Completeness [%] | 99.8 | 99.9 |
Redundancy | 7.1 | 6.9 |
CC(1/2) | 0.999 | 0.721 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 285 | PEG 3000 - 6000 15-24 % (w/v) Bicine buffer 0.1 M |