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) |