6MOP
Crystal Structure of the All-trans Retinal-Bound R111K:Y134F:T54V:R132Q:P39Y:R59Y:L121E Mutant of Human Cellular Retinoic Acid Binding Protein II in the Dark at 1.9 Angstrom Resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-G |
Synchrotron site | APS |
Beamline | 21-ID-G |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2016-10-12 |
Detector | RAYONIX MX300HE |
Wavelength(s) | 0.97856 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 58.986, 58.986, 100.314 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 35.789 - 1.900 |
R-factor | 0.1975 |
Rwork | 0.195 |
R-free | 0.22770 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4yfp |
RMSD bond length | 0.007 |
RMSD bond angle | 0.869 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX |
Refinement software | PHENIX ((1.14_3260)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 35.789 | 1.930 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.050 | 0.050 |
Rmeas | 0.072 | |
Rpim | 0.027 | 0.367 |
Number of reflections | 16473 | 1618 |
<I/σ(I)> | 34.4 | |
Completeness [%] | 100.0 | |
Redundancy | 7.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 277 | PEG 3350, DL-malic acid |