4JQI
Structure of active beta-arrestin1 bound to a G protein-coupled receptor phosphopeptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 78 |
| Detector technology | CCD |
| Collection date | 2012-07-28 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.033 |
| Spacegroup name | I 21 21 21 |
| Unit cell lengths | 116.840, 125.128, 144.203 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.281 - 2.600 |
| R-factor | 0.2029 |
| Rwork | 0.201 |
| R-free | 0.24660 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1jsy 3eff |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.785 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.8.1_1168)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.300 | 2.700 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Number of reflections | 32184 | |
| <I/σ(I)> | 2.1 | |
| Completeness [%] | 98.1 | 97.5 |
| Redundancy | 5.8 | 5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | 17% PEG 3350, 0.1 M HEPES, 0.2 M L-proline , pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
