4P6Q
The crystal structure of the Split End protein SHARP adds a new layer of complexity to proteins containing RNA Recognition Motifs
Experimental procedure
| Experimental method | SINGLE WAVELENGTH | 
| Source type | SYNCHROTRON | 
| Source details | ESRF BEAMLINE BM16 | 
| Synchrotron site | ESRF | 
| Beamline | BM16 | 
| Temperature [K] | 100 | 
| Detector technology | CCD | 
| Collection date | 2012-11-29 | 
| Detector | ADSC QUANTUM 315r | 
| Wavelength(s) | 1.0 | 
| Spacegroup name | P 21 21 21 | 
| Unit cell lengths | 60.670, 69.710, 88.920 | 
| Unit cell angles | 90.00, 90.00, 90.00 | 
Refinement procedure
| Resolution | 28.710 - 2.000 | 
| R-factor | 0.1959 | 
| Rwork | 0.192 | 
| R-free | 0.23770 | 
| Structure solution method | MOLECULAR REPLACEMENT | 
| Starting model (for MR) | Ensemble 1 (PDB codes: 3MD1 2adc 2dnm 2dgu 2CQB); Ensemble 2 (PDB codes: X4AR 2ytc 4f26 1why 2CPZ); Ensemble 3 (PDB codes: 2I38 1why 1x55 2lcw 2CPE). | 
| RMSD bond length | 0.008 | 
| RMSD bond angle | 1.096 | 
| Data reduction software | XDS | 
| Data scaling software | XSCALE | 
| Phasing software | PHASER | 
| Refinement software | PHENIX ((phenix.refine: 1.8.1_1168)) | 
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 28.710 | |
| High resolution limit [Å] | 2.000 | 2.000 | 
| Number of reflections | 26164 | |
| <I/σ(I)> | 20.44 | |
| Completeness [%] | 99.7 | 100 | 
| Redundancy | 5.38 | 5.63 | 
Crystallization Conditions
| crystal ID | method | pH | temperature | details | 
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.6 | 277 | 15% PEG 8000, 0.1M ammonium sulphate, 0.01M magnesium chloride, 0.05M 2-(N-morpholino)ethanesulfonic acid | 











