7RRY
Crystal Structure of the ER-alpha Ligand-binding Domain (L372S, L536S) in complex with DMERI-20
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-10-18 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 |
| Unit cell lengths | 53.416, 59.119, 93.522 |
| Unit cell angles | 86.54, 74.98, 63.19 |
Refinement procedure
| Resolution | 90.130 - 1.870 |
| R-factor | 0.2087 |
| Rwork | 0.207 |
| R-free | 0.23560 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2qxs |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.466 |
| Data reduction software | AutoProcess |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0253) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 90.134 | 2.045 |
| High resolution limit [Å] | 1.869 | 1.869 |
| Number of reflections | 61892 | 2861 |
| <I/σ(I)> | 7.5 | 1.4 |
| Completeness [%] | 76.0 | |
| Redundancy | 6.9 | |
| CC(1/2) | 0.990 | 0.490 |
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 |
