3FFA
Crystal Structure of a fast activating G protein mutant
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-C |
Synchrotron site | APS |
Beamline | 24-ID-C |
Temperature [K] | 298 |
Detector technology | CCD |
Collection date | 2006-11-06 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.973 |
Spacegroup name | P 32 2 1 |
Unit cell lengths | 79.008, 79.008, 105.667 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 57.400 - 2.300 |
R-factor | 0.18809 |
Rwork | 0.185 |
R-free | 0.25157 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1as0 |
RMSD bond length | 0.022 |
RMSD bond angle | 1.876 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 57.400 | 2.400 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.083 | 0.220 |
Number of reflections | 17460 | |
<I/σ(I)> | 7.3 | |
Completeness [%] | 100.0 | 100 |
Redundancy | 5.3 | 5.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 6 | 293 | 100 mM Sodium Acetate pH 5.9-6.3, 1.8-2.1 M Ammonium Sulphate, VAPOR DIFFUSION, temperature 293K, pH 6.0 |