4I7D
Siah1 bound to synthetic peptide (ACE)KLRPVAMVRP(PRK)VR
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL12-2 |
| Synchrotron site | SSRL |
| Beamline | BL12-2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2012-03-15 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.979 |
| Spacegroup name | I 2 3 |
| Unit cell lengths | 160.977, 160.977, 160.977 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.400 |
| R-factor | 0.17296 |
| Rwork | 0.171 |
| R-free | 0.20167 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2A25 CHAIN A |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.030 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.440 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.073 | 0.662 |
| Number of reflections | 27179 | |
| <I/σ(I)> | 22.2 | 2.2 |
| Completeness [%] | 99.8 | 99.8 |
| Redundancy | 5.1 | 5.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 9 | 293 | 65% MPD, 100 mM bicine, pH 9.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
