1E0S
small G protein Arf6-GDP
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | LURE BEAMLINE DW32 |
Synchrotron site | LURE |
Beamline | DW32 |
Temperature [K] | 277 |
Detector technology | IMAGE PLATE |
Detector | MARRESEARCH |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 55.660, 55.660, 194.950 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.000 - 2.280 |
R-factor | 0.172 |
Rwork | 0.172 |
R-free | 0.23400 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1hur |
RMSD bond length | 0.015 |
RMSD bond angle | 2.211 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | X-PLOR (98) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.360 |
High resolution limit [Å] | 2.280 | 2.280 |
Rmerge | 0.064 * | 0.152 * |
Total number of observations | 76362 * | |
Number of reflections | 8748 | |
<I/σ(I)> | 12.8 | |
Completeness [%] | 98.5 | 98.5 |
Redundancy | 5.5 | 5.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8.5 | 4 * | 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 | 5.8 (mg/ml) | |
2 | 1 | reservoir | ammonium sulfate | 2 (M) | |
3 | 1 | reservoir | Tris-HCl | 0.1 (M) |