3EQ5
Crystal structure of fragment 137 to 238 of the human Ski-like protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-07-25 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97623 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 210.820, 70.120, 116.280 |
| Unit cell angles | 90.00, 100.95, 90.00 |
Refinement procedure
| Resolution | 19.830 - 2.450 |
| R-factor | 0.23449 |
| Rwork | 0.232 |
| R-free | 0.27428 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1sbx |
| RMSD bond length | 0.006 |
| RMSD bond angle | 0.808 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0035) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 19.830 | 2.510 |
| High resolution limit [Å] | 2.450 | 2.450 |
| Rmerge | 0.074 | 0.597 |
| Number of reflections | 60345 | |
| <I/σ(I)> | 12 | 2.26 |
| Completeness [%] | 97.8 | 98.7 |
| Redundancy | 2.6 | 2.63 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 277 | 20% PEG 3350, 0.2M Ammonium nitrate, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
