6QBO
structure of the core domaine of Knr4, an intrinsically disordered protein from Saccharomyces cerevisiae - mutant 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 | 2016-01-29 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 1.072274 |
Spacegroup name | P 62 |
Unit cell lengths | 103.104, 103.104, 93.565 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 45.190 - 2.750 |
R-factor | 0.1867 |
Rwork | 0.185 |
R-free | 0.21355 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5j1b |
RMSD bond length | 0.007 |
RMSD bond angle | 1.105 |
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] | 45.200 | 2.800 |
High resolution limit [Å] | 2.750 | 2.750 |
Rmeas | 0.074 | 1.488 |
Number of reflections | 14760 | 765 |
<I/σ(I)> | 14.4 | 1.1 |
Completeness [%] | 99.8 | 98.2 |
Redundancy | 5.7 | 5 |
CC(1/2) | 0.999 | 0.325 |
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 |