6MR0
Crystal Structure of the All-trans Retinal Bound R111K:Y134F:T54V:R132Q:P39Q:R59Y:L121E Human Cellular Retinoic Acid Binding Protein II Mutant After 5 Minutes UV irradiation at 2.6 Angstrom Resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2018-01-01 |
| Detector | RAYONIX MX300HE |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 31 2 1 |
| Unit cell lengths | 58.476, 58.476, 99.552 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 35.499 - 2.649 |
| R-factor | 0.1996 |
| Rwork | 0.191 |
| R-free | 0.27360 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4yfp |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.005 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.14_3260)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 35.499 | 2.744 |
| High resolution limit [Å] | 2.649 | 2.650 |
| Rmerge | 0.150 | 0.800 |
| Rpim | 0.324 | |
| Number of reflections | 6063 | 569 |
| <I/σ(I)> | 11.25 | 2 |
| Completeness [%] | 99.6 | 97.43 |
| Redundancy | 10.7 | 10.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 277 | PEG 3350, BTP, Sodium Fluoride |
