4XOF
Observing the overall rocking motion of a protein in a crystal - Orthorhombic Ubiquitin crystals without Zinc.
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 | 2014-10-07 |
| Detector | DECTRIS PILATUS 2M |
| Wavelength(s) | 0.873 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 27.940, 43.300, 50.190 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 32.780 - 1.150 |
| R-factor | 0.1386 |
| Rwork | 0.137 |
| R-free | 0.17130 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3ehv |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.269 |
| 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] | 32.780 | 1.191 |
| High resolution limit [Å] | 1.150 | 1.150 |
| Rmerge | 0.061 | 0.811 |
| Number of reflections | 22230 | |
| <I/σ(I)> | 14.1 | 1.93 |
| Completeness [%] | 99.7 | 98.12 |
| Redundancy | 7 | 6.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 | 25% (w/v) PEG 1450, 50mM HEPES pH 7.0 |
