5AMO
Structure of a mouse Olfactomedin-1 disulfide-linked dimer of the Olfactomedin domain and part of the coiled coil
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2013-11-08 |
| Detector | DECTRIS PILATUS 6M |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 160.220, 43.940, 104.060 |
| Unit cell angles | 90.00, 114.17, 90.00 |
Refinement procedure
| Resolution | 50.318 - 2.400 |
| R-factor | 0.238 |
| Rwork | 0.237 |
| R-free | 0.25780 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4d77 |
| RMSD bond length | 0.002 |
| RMSD bond angle | 0.555 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 95.000 | 2.500 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.080 | 0.780 |
| Number of reflections | 26050 | |
| <I/σ(I)> | 7.7 | 1.2 |
| Completeness [%] | 98.9 | 99.4 |
| Redundancy | 3.4 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | SITTING DROP AT 293 K, MIXING PROTEIN AT 6 MG/ML 1:1 WITH PRECIPITANT SOLUTION: 1M LICL, 20% PEG6000 (W/V) AND 100 MM TRIS PH8.5 |
