5H9A
Crystal structure of the Apo form of human cellular retinol binding protein 1
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-C |
| Synchrotron site | APS |
| Beamline | 24-ID-C |
| Temperature [K] | 80 |
| Detector technology | PIXEL |
| Collection date | 2015-08-01 |
| Detector | DECTRIS PILATUS 6M-F |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 37.350, 37.960, 94.960 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 35.248 - 1.381 |
| R-factor | 0.1351 |
| Rwork | 0.133 |
| R-free | 0.17130 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1crb |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.123 |
| Data reduction software | iMOSFLM |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (1.10pre_2138) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 35.248 | 1.410 |
| High resolution limit [Å] | 1.380 | 1.380 |
| Rmerge | 0.598 | |
| Number of reflections | 28067 | |
| <I/σ(I)> | 11 | 2.8 |
| Completeness [%] | 98.9 | 98.9 |
| Redundancy | 5.3 | 4.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 298 | 0.1 M Bis-Tris, 25% PEG 6000 |
