7RS7
Crystal Structure of the ER-alpha Ligand-binding Domain (L372S, L536S) in complex with DMERI-30
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 | 2019-07-02 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 |
| Unit cell lengths | 53.665, 58.621, 93.932 |
| Unit cell angles | 87.27, 74.87, 62.91 |
Refinement procedure
| Resolution | 90.370 - 1.580 |
| R-factor | 0.2246 |
| Rwork | 0.223 |
| R-free | 0.25100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2qxs |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.522 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0253) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 90.370 | 1.639 |
| High resolution limit [Å] | 1.580 | 1.580 |
| Number of reflections | 89258 | 3316 |
| <I/σ(I)> | 4 | |
| Completeness [%] | 86.7 | |
| Redundancy | 7.3 | |
| CC(1/2) | 0.987 | 0.475 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 298 | 20-25% PEG 3350, 200 mM MgCl2, 0.1 M Bis-Tris/Hepes/Tris-HCl |
