5E94
Antibody-bound Glucagon-like Peptide-1 receptor extracellular domain
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I911-3 |
| Synchrotron site | MAX II |
| Beamline | I911-3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-06-22 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 1 |
| Unit cell lengths | 57.201, 65.692, 88.351 |
| Unit cell angles | 111.61, 97.47, 91.28 |
Refinement procedure
| Resolution | 32.090 - 2.000 |
| R-factor | 0.1902 |
| Rwork | 0.188 |
| R-free | 0.23230 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3IOL and 1BZ7 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.121 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX (dev_1938) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 32.000 | 2.070 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.039 | 0.225 |
| Number of reflections | 72374 | |
| <I/σ(I)> | 13.9 | 3.8 |
| Completeness [%] | 90.0 | 95 |
| Redundancy | 1.7 | 1.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 291 | 0.2 M Sodium dihydrogen Phosphate monohydrate, 20% w/v PEG 3350 |
