4LLO
Structure of the eag domain-CNBHD complex of the mouse EAG1 channel
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.1 |
| Synchrotron site | ALS |
| Beamline | 8.2.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-09-24 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 65 |
| Unit cell lengths | 162.380, 162.380, 100.440 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 42.710 - 1.995 |
| R-factor | 0.1684 |
| Rwork | 0.167 |
| R-free | 0.19740 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4f8a |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.043 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: dev_1269)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 42.710 | 2.100 |
| High resolution limit [Å] | 1.995 | 2.000 |
| Rmerge | 0.160 | 0.729 |
| Number of reflections | 102374 | |
| <I/σ(I)> | 9.5 | 2.7 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 11.8 | 9.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293.15 | 18% (w/v) PEG 3350, 1.8% (v/v) Tacsimate, 0.01M MnCl2 and 0.09M HEPES, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K |






