3ONW
Structure of a G-alpha-i1 mutant with enhanced affinity for the RGS14 GoLoco motif.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-BM |
Synchrotron site | APS |
Beamline | 22-BM |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2009-11-30 |
Detector | MAR scanner 300 mm plate |
Wavelength(s) | 1.000 |
Spacegroup name | P 2 2 21 |
Unit cell lengths | 70.392, 83.679, 190.148 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 95.070 - 2.380 |
R-factor | 0.22953 |
Rwork | 0.228 |
R-free | 0.26539 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2OM2 chain A |
RMSD bond length | 0.009 |
RMSD bond angle | 1.086 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 28.880 | 2.400 |
High resolution limit [Å] | 2.380 | 2.380 |
Rmerge | 0.065 | 0.761 |
Number of reflections | 45328 | |
<I/σ(I)> | 27.3 | 2.2 |
Completeness [%] | 98.8 | 100 |
Redundancy | 6 | 6 |
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 (1.9 M ammonium sulfate, 100 mM sodium acetate pH 5.0, 200 mM magnesium chloride, 10% (w/v) glycerol), VAPOR DIFFUSION, HANGING DROP, temperature 291K |