1BYW
STRUCTURE OF THE N-TERMINAL DOMAIN OF THE HUMAN-ERG POTASSIUM CHANNEL
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | CHESS BEAMLINE F2 |
| Synchrotron site | CHESS |
| Beamline | F2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Wavelength(s) | 0.9793, 0.97896, 0.973 |
| Spacegroup name | P 65 2 2 |
| Unit cell lengths | 56.100, 56.100, 135.500 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 13.000 - 2.600 |
| R-factor | 0.252 |
| Rwork | 0.252 |
| R-free | 0.28600 |
| Structure solution method | MAD |
| RMSD bond length | 0.004 |
| RMSD bond angle | 26.420 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | CCP4 |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 13.000 | 2.700 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.092 * | 0.354 * |
| Number of reflections | 4131 | |
| <I/σ(I)> | 34 | 5 |
| Completeness [%] | 95.8 | 87.9 |
| Redundancy | 7 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 8 * | 20 * | drop consists of equal volume of protein and reservoir solutions * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | dithiothreitol | 10 (mM) | |
| 3 | 1 | drop | n-octyl-beta-D-glucoside | 5 (mM) | |
| 4 | 1 | drop | 150 (mM) | ||
| 5 | 1 | drop | Tris-HCl | 50 (mM) | |
| 6 | 1 | reservoir | sodium and potassium tartrate | 0.8-1.0 (M) | |
| 7 | 1 | reservoir | HEPES | 100 (mM) |
