6QBP
structure of the core domaine of Knr4, an intrinsically disordered protein from Saccharomyces cerevisiae - mutant S203D
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-1 |
Synchrotron site | ESRF |
Beamline | ID23-1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2015-10-21 |
Detector | DECTRIS PILATUS3 6M |
Wavelength(s) | 0.976256 |
Spacegroup name | P 62 |
Unit cell lengths | 102.949, 102.949, 93.139 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 45.090 - 2.400 |
R-factor | 0.19216 |
Rwork | 0.191 |
R-free | 0.21863 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5j1b |
RMSD bond length | 0.006 |
RMSD bond angle | 1.028 |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0230) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 89.170 | 2.540 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmeas | 0.043 | 1.115 |
Number of reflections | 21807 | 3415 |
<I/σ(I)> | 17.6 | 1 |
Completeness [%] | 99.1 | 97.2 |
Redundancy | 3.5 | 2.5 |
CC(1/2) | 0.999 | 0.371 |
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 |