3C5T
Crystal structure of the ligand-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 | 2006-11-14 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 1.00 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 75.910, 75.910, 87.770 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 36.500 - 2.100 |
| R-factor | 0.20503 |
| Rwork | 0.203 |
| R-free | 0.23809 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3C59 without the ligand present |
| RMSD bond length | 0.019 |
| RMSD bond angle | 1.702 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.3.0040) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.200 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.061 | 0.395 |
| Number of reflections | 17273 | |
| <I/σ(I)> | 27.1 | 7.3 |
| Completeness [%] | 98.3 | 97.8 |
| Redundancy | 10.9 | 11.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 293 | 0.1M Tris-HCl pH 8.5, 0.1M MgCl2, 0.4M MgTartrate, 9mM n-Decyl-beta-D-thiomaltoside, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
