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 |
