1XHM
The Crystal Structure of a Biologically Active Peptide (SIGK) Bound to a G Protein Beta:Gamma Heterodimer
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.2 |
| Synchrotron site | ALS |
| Beamline | 8.2.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-11-18 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.0871 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 45.468, 74.669, 108.023 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 41.910 - 2.700 |
| R-factor | 0.227 |
| Rwork | 0.227 |
| R-free | 0.28700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1omw |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.300 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.800 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.414 | |
| Number of reflections | 9729 | |
| <I/σ(I)> | 13.5 | 1.6 |
| Completeness [%] | 88.3 | 38.6 |
| Redundancy | 3.5 | 1.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | PEG 4000, GLYCEROL, HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
