6MCV
Crystal Structure of Holo Retinal-Bound Domain-Swapped Dimer of Wild Type 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 | 2016-11-26 |
Detector | RAYONIX MX300HE |
Wavelength(s) | 0.97872 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 65.819, 74.362, 352.547 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 14.993 - 3.300 |
R-factor | 0.2098 |
Rwork | 0.208 |
R-free | 0.26580 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2rct |
RMSD bond length | 0.001 |
RMSD bond angle | 0.348 |
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] | 14.993 | 3.360 |
High resolution limit [Å] | 3.300 | 3.300 |
Rmerge | 0.190 | |
Rmeas | 0.200 | |
Rpim | 0.303 | |
Number of reflections | 24088 | 2395 |
<I/σ(I)> | 17.1 | |
Completeness [%] | 89.8 | 92.12 |
Redundancy | 10.5 | |
CC(1/2) | 0.773 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 298 | 4000 PEG, Ammonium acetate, Sodium acetate |