5TDH
The crystal structure of the dominant negative mutant G protein alpha(i)-1-beta-1-gamma-2 G203A/A326S
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRF BEAMLINE BL17U |
Synchrotron site | SSRF |
Beamline | BL17U |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2015-12-22 |
Detector | MAR scanner 345 mm plate |
Wavelength(s) | 0.97915 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 126.009, 54.570, 138.350 |
Unit cell angles | 90.00, 113.10, 90.00 |
Refinement procedure
Resolution | 43.635 - 3.000 |
R-factor | 0.2783 |
Rwork | 0.276 |
R-free | 0.30530 |
RMSD bond length | 0.003 |
RMSD bond angle | 0.727 |
Data reduction software | iMOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 3.000 |
Number of reflections | 34720 |
<I/σ(I)> | 5.7 |
Completeness [%] | 98.4 |
Redundancy | 6.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 5.6 | 293 | 2% v/v Tacsimate (pH 5.0), 0.1 M sodium citrate tribasic dehydrate (pH 5.6), 16% w/v PEG 3350 |