5HA1
Crystal structure of human cellular retinol binding protein 1 in complex with retinylamine
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] | 90 |
| Detector technology | CCD |
| Collection date | 2015-08-01 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 37.150, 49.570, 73.300 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 27.548 - 1.350 |
| R-factor | 0.1237 |
| Rwork | 0.122 |
| R-free | 0.15570 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1crb |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.131 |
| 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] | 27.550 | 1.350 |
| High resolution limit [Å] | 1.350 | 1.320 |
| Rmerge | 0.604 | |
| Number of reflections | 30442 | |
| <I/σ(I)> | 9.4 | 3.2 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 5.9 | 5.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 298 | 0.1 M Bis-Tris, 25% PEG 6000 |
