4I7B
Siah1 bound to synthetic peptide (ACE)KLRPV(ABA)MVRPTVR
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL9-2 |
| Synchrotron site | SSRL |
| Beamline | BL9-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-03-28 |
| Detector | MARMOSAIC 325 mm CCD |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 39.745, 87.913, 59.884 |
| Unit cell angles | 90.00, 100.59, 90.00 |
Refinement procedure
| Resolution | 35.700 - 3.000 |
| R-factor | 0.18951 |
| Rwork | 0.186 |
| R-free | 0.26051 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2A25 CHAIN A |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.907 |
| 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 | 3.110 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.077 | 0.600 |
| Number of reflections | 8152 | |
| <I/σ(I)> | 25.1 | 2.5 |
| Completeness [%] | 99.5 | 97.7 |
| Redundancy | 3.7 | 3.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 10% PEG6000, 5% MPD, 100 mM HEPES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
