6E5E
Crystal structure of the apo domain-swapped dimer Q108K:T51D 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 | 2015-10-16 |
| Detector | RAYONIX MX300HE |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 60.218, 63.757, 36.739 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 36.739 - 1.696 |
| R-factor | 0.2081 |
| Rwork | 0.204 |
| R-free | 0.24240 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2rcq |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.834 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.11.1_2575)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 36.740 | 1.757 |
| High resolution limit [Å] | 1.696 | 1.696 |
| Rmerge | 0.220 | 0.920 |
| Rmeas | 0.100 | |
| Number of reflections | 16292 | |
| <I/σ(I)> | 10.6 | 2.3 |
| Completeness [%] | 99.7 | |
| Redundancy | 3.9 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 298 | 4000 PEG, sodium acetate, ammonium acetate |
