5EPQ
Structure at 1.75 A resolution of a glycosylated, lipid-binding, lipocalin-like protein
Replaces: 4NYSExperimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SOLEIL BEAMLINE PROXIMA 1 |
| Synchrotron site | SOLEIL |
| Beamline | PROXIMA 1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2015-07-21 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 1 |
| Unit cell lengths | 32.221, 33.321, 39.919 |
| Unit cell angles | 99.22, 99.97, 103.76 |
Refinement procedure
| Resolution | 38.434 - 1.752 |
| R-factor | 0.1842 |
| Rwork | 0.182 |
| R-free | 0.21480 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4nyq |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.938 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.860 |
| High resolution limit [Å] | 1.750 | 1.750 |
| Rmerge | 0.136 | 0.373 |
| Number of reflections | 15194 | |
| <I/σ(I)> | 3.97 | 1.67 |
| Completeness [%] | 95.1 | 90.8 |
| Redundancy | 1.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 | PEG 10000 |
