6QBN
structure of the core domaine of Knr4, an intrinsically disordered protein from Saccharomyces cerevisiae - mutant S200D
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 | 103.110, 103.110, 93.390 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 45.180 - 2.400 |
R-factor | 0.18175 |
Rwork | 0.180 |
R-free | 0.21691 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5j1b |
RMSD bond length | 0.015 |
RMSD bond angle | 1.660 |
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] | 89.300 | 2.460 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmeas | 1.345 | |
Number of reflections | 20213 | 1121 |
<I/σ(I)> | 0.046 | 1.3 |
Completeness [%] | 95.3 | 68.9 |
Redundancy | 8 | 5.8 |
CC(1/2) | 1.000 | 0.460 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 285 | PEG 3000 - 6000 15-24 % (w/v) Bicine buffer 0.1 M |