6AT8
1.1 Angstrom Resolution Structure of Human Cellular Retinol-Binding Protein IV
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-E |
| Synchrotron site | APS |
| Beamline | 24-ID-E |
| Temperature [K] | 80 |
| Detector technology | PIXEL |
| Collection date | 2017-08-20 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.97919 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 34.820, 57.334, 68.115 |
| Unit cell angles | 90.00, 103.09, 90.00 |
Refinement procedure
| Resolution | 29.190 - 1.105 |
| R-factor | 0.1267 |
| Rwork | 0.126 |
| R-free | 0.14920 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1lpj |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.971 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.10.1_2155) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 29.190 | 1.160 |
| High resolution limit [Å] | 1.105 | 1.105 |
| Rmerge | 0.053 | |
| Rmeas | 0.035 | 0.090 |
| Rpim | 0.026 | 0.077 |
| Number of reflections | 49226 | 5474 |
| <I/σ(I)> | 31.8 | 8.6 |
| Completeness [%] | 94.4 | 72 |
| Redundancy | 5.5 | |
| CC(1/2) | 0.994 | 0.982 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 295 | 0.2 M NaCl, 0.1 M Bis-Tris/HCl, 25% PEG3350 (w/v) |






