2BT2
Structure of the regulator of G-protein signaling 16
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SLS BEAMLINE X10SA |
| Synchrotron site | SLS |
| Beamline | X10SA |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-04-23 |
| Detector | MARRESEARCH |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 160.585, 31.743, 151.766 |
| Unit cell angles | 90.00, 94.39, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.900 |
| R-factor | 0.195 |
| Rwork | 0.192 |
| R-free | 0.25000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1agr |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.404 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 44.230 | 2.000 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.080 | 0.450 |
| Number of reflections | 216171 | |
| <I/σ(I)> | 9.5 | 2.39 |
| Completeness [%] | 95.6 | 85.2 |
| Redundancy | 3.32 | 2.66 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.5 | 0.1 M BIS-TRIS, PH 5.5, 26% PEG3350, 0.1 M NH4AC |
