3QE0
A Galpha-i1 P-loop mutation prevents transition to the activated state
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 | 2010-10-01 |
Detector | MAR scanner 300 mm plate |
Wavelength(s) | 1.000 |
Spacegroup name | P 61 2 2 |
Unit cell lengths | 106.637, 106.637, 455.062 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 39.441 - 3.000 |
R-factor | 0.2491 |
Rwork | 0.247 |
R-free | 0.29170 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1y3a |
RMSD bond length | 0.002 |
RMSD bond angle | 0.546 |
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] | 39.441 | 3.030 |
High resolution limit [Å] | 3.000 | 3.000 |
Number of reflections | 30772 | |
<I/σ(I)> | 2 | |
Completeness [%] | 96.7 | 85.4 |
Redundancy | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 291 | Hanging drops were a 1:1 mixture of protein-peptide complex in buffer (50 mM HEPES pH 8.0, 10 mM magnesium chloride, 10 microM GppNHp, 1 mM EDTA, 5 mM DTT) and well solution (17% (w/v) PEG MME 5K, 200 mM magnesium chloride, 100 mM HEPES pH 7.0), VAPOR DIFFUSION, HANGING DROP, temperature 291K |