6QBM
structure of the core domaine of Knr4, an intrinsically disordered protein from Saccharomyces cerevisiae - mutant S200A
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 | 103.004, 103.004, 93.379 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 45.100 - 2.500 |
| R-factor | 0.19335 |
| Rwork | 0.191 |
| R-free | 0.23665 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5j1b |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.060 |
| 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] | 45.140 | 2.650 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmeas | 0.041 | |
| Number of reflections | 19631 | 3158 |
| <I/σ(I)> | 19.2 | |
| Completeness [%] | 99.9 | 99.6 |
| Redundancy | 4.5 | 4.7 |
| CC(1/2) | 1.000 | 0.290 |
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 |
