2DX1
Crystal structure of RhoGEF protein Asef
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL44B2 |
Synchrotron site | SPring-8 |
Beamline | BL44B2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-06-07 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9789, 0.9794, 0.9640 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 100.932, 79.818, 68.004 |
Unit cell angles | 90.00, 123.25, 90.00 |
Refinement procedure
Resolution | 34.610 - 2.360 |
Rwork | 0.232 |
R-free | 0.29900 |
Structure solution method | MAD |
RMSD bond length | 0.010 |
RMSD bond angle | 1.300 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SOLVE |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.440 |
High resolution limit [Å] | 2.360 | 2.360 |
Number of reflections | 18703 | |
Completeness [%] | 99.9 | 100 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 20% PEG3350, 0.2M MgCl2, 0.1M HEPES-HCl buffer, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |