1GG2
G PROTEIN HETEROTRIMER MUTANT GI_ALPHA_1(G203A) BETA_1 GAMMA_2 WITH GDP BOUND
Experimental procedure
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE A1 |
Synchrotron site | CHESS |
Beamline | A1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1996-01 |
Spacegroup name | P 43 |
Unit cell lengths | 83.776, 83.776, 130.938 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 15.000 - 2.400 |
R-factor | 0.205 |
Rwork | 0.205 |
R-free | 0.28900 |
Structure solution method | REFINEMENT WITH WILD-TYPE MODEL (SAME CELL) |
RMSD bond length | 0.011 |
RMSD bond angle | 24.300 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 2.490 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.073 | 0.301 |
Number of reflections | 32774 | |
<I/σ(I)> | 11.4 | 2.28 |
Completeness [%] | 93.0 | 91 |
Redundancy | 2.55 | 2.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7 | 21 * | pH 7.0 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG8000 | 18 (%) | |
2 | 1 | reservoir | Na-HEPES | 100 (mM) | pH7.0 |
3 | 1 | reservoir | sodium acetate | 100 (mM) | pH6.4 |
4 | 1 | reservoir | n-beta-octyl-glucoside | 0.05 (%) | |
5 | 1 | reservoir | 2-propanol | 2 (%) | |
6 | 1 | drop | protein | 7.5 (mg/ml) |