3V00
Studies of a constitutively active G-alpha subunit provide insights into the mechanism of G protein activation.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE A1 |
Synchrotron site | CHESS |
Beamline | A1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2007-11-08 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.978 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 93.173, 93.173, 380.580 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 39.740 - 2.900 |
R-factor | 0.221 |
Rwork | 0.221 |
R-free | 0.27200 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1tag |
RMSD bond length | 0.007 |
RMSD bond angle | 1.100 |
Data reduction software | DENZO |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 39.740 | 2.800 |
High resolution limit [Å] | 2.700 | 2.700 |
Rmerge | 0.080 | |
Number of reflections | 47006 | |
<I/σ(I)> | 21.253 | |
Completeness [%] | 99.2 | 8.8 |
Redundancy | 8.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.3 | 295 | 1.9 M Ammonium Sulphate in 0.05 M Sodium Cacodylate buffer, pH 6.3, VAPOR DIFFUSION, HANGING DROP, temperature 295K |