6E50
Crystal structure of the apo domain-swapped dimer Q108K:K40L:T51F mutant of human Cellular Retinol Binding Protein II
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 | 2016-06-05 |
| Detector | RAYONIX MX300HE |
| Wavelength(s) | 0.97856 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 63.637, 60.468, 36.659 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.120 - 1.965 |
| R-factor | 0.2077 |
| Rwork | 0.201 |
| R-free | 0.26600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2rcq |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.889 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((1.11.1_2575)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 28.120 | 2.036 |
| High resolution limit [Å] | 1.965 | 1.965 |
| Rmerge | 0.057 | 0.430 |
| Rmeas | 0.067 | 0.505 |
| Number of reflections | 8891 | 879 |
| <I/σ(I)> | 23.78 | |
| Completeness [%] | 84.0 | 85.7 |
| Redundancy | 3.2 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 298 | PEG 4000, sodium acetate, Ammonium acetate |
