6QBR
structure of the core domaine of Knr4, an intrinsically disordered protein from Saccharomyces cerevisiae - mutant S200D, S203D
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 | 102.380, 102.380, 92.336 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 44.810 - 2.150 |
| R-factor | 0.19228 |
| Rwork | 0.191 |
| R-free | 0.21852 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5j1b |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.256 |
| 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 | 2.280 |
| High resolution limit [Å] | 2.150 | 2.150 |
| Rmeas | 0.068 | 0.959 |
| Number of reflections | 29991 | 4716 |
| <I/σ(I)> | 13.3 | 1.1 |
| Completeness [%] | 99.5 | 97 |
| Redundancy | 5.2 | 3.3 |
| CC(1/2) | 0.997 | 0.520 |
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 |
