4I7C
Siah1 mutant bound to synthetic peptide (ACE)KLRPV(23P)MVRPWVR
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 | 2012-05-24 |
| Detector | MARMOSAIC 325 mm CCD |
| Wavelength(s) | 0.979 |
| Spacegroup name | I 2 3 |
| Unit cell lengths | 164.230, 164.230, 164.230 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.800 |
| R-factor | 0.18052 |
| Rwork | 0.178 |
| R-free | 0.21920 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4i7d |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.163 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 60.000 | 2.950 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.123 | 1.637 |
| Number of reflections | 18317 | |
| <I/σ(I)> | 12.1 | 1.5 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 11.4 | 11.4 |
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 |
