6RMV
The crystal structure of a TRP channel peptide bound to a G protein beta gamma heterodimer
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID30B |
| Synchrotron site | ESRF |
| Beamline | ID30B |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-10-23 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.9754 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 45.860, 80.432, 113.587 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 42.520 - 1.940 |
| R-factor | 0.1896 |
| Rwork | 0.188 |
| R-free | 0.22430 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1xhm |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.211 |
| Data reduction software | XDS |
| Data scaling software | Aimless (0.5.32) |
| Phasing software | PHASER (2.7.17) |
| Refinement software | REFMAC (5.8.0158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 42.520 | 2.010 |
| High resolution limit [Å] | 1.940 | 1.940 |
| Rmerge | 0.073 | 1.280 |
| Rmeas | 0.087 | 1.510 |
| Rpim | 0.046 | 0.795 |
| Number of reflections | 31659 | 3044 |
| <I/σ(I)> | 13.2 | 1.4 |
| Completeness [%] | 99.3 | 98.3 |
| Redundancy | 6.5 | 6.7 |
| CC(1/2) | 0.999 | 0.528 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 291.15 | 0.1 M HEPES sodium pH 7.5, 15% (w/v) polyethylene glycol 4,000, 7.5% (v/v) isopropanol |






