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 |






