4XOL
Observing the overall rocking motion of a protein in a crystal - Cubic Ubiquitin crystals.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-2 |
| Synchrotron site | ESRF |
| Beamline | ID23-2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2014-11-07 |
| Detector | DECTRIS PILATUS 2M |
| Wavelength(s) | 0.873 |
| Spacegroup name | P 43 3 2 |
| Unit cell lengths | 104.946, 104.946, 104.946 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 34.980 - 2.910 |
| R-factor | 0.2399 |
| Rwork | 0.237 |
| R-free | 0.26870 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3n30 |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.933 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.9_1692)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 34.980 | 3.013 |
| High resolution limit [Å] | 2.910 | 2.910 |
| Rmerge | 0.777 | |
| Number of reflections | 4656 | |
| <I/σ(I)> | 16.46 | 2.11 |
| Completeness [%] | 98.8 | 99.34 |
| Redundancy | 5.1 | 5.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.33 | 293 | 100mM MES pH 6.33, 20% PEG 3350, 100mM Zn Acetate. |
