3QI2
A Galpha P-loop mutation prevents transition to the activated state: G42R bound to RGS14 GoLoco
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2010-11-01 |
Detector | MAR scanner 300 mm plate |
Wavelength(s) | 1.000 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 70.003, 131.018, 203.307 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.705 - 2.797 |
R-factor | 0.2001 |
Rwork | 0.196 |
R-free | 0.27260 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2om2 |
RMSD bond length | 0.002 |
RMSD bond angle | 0.463 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.6_289)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.705 | 2.944 |
High resolution limit [Å] | 2.797 | 2.797 |
Number of reflections | 18462 | |
<I/σ(I)> | 2 | 2 |
Completeness [%] | 78.4 | 31 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5 | 291 | Hanging drops were a 1:1 mixture of protein-peptide complex in buffer (10 mM Tris pH 7.5, 1 mM magnesium chloride, 5% (w/v) glycerol, 5 mM DTT) and well solution (1.7 M ammonium sulfate, 100 mM sodium acetate pH 5.0, 200 mM magnesium chloride, 10% (w/v) glycerol), VAPOR DIFFUSION, HANGING DROP, temperature 291K |