6MQZ
Crystal Structure of the 13-cis Product of the All-trans Retinal-Bound R111K:Y134F:T54V:R132Q:P39Y:R59Y:L121E Mutant of Human Cellular Retinoic Acid Binding Protein II Irradiated with 400 nm Laser (5 minutes) at 2.07 Angstrom
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 | 2016-10-25 |
Detector | RAYONIX MX300HE |
Wavelength(s) | 0.97872 |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 58.567, 58.567, 98.974 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 45.139 - 2.070 |
R-factor | 0.1983 |
Rwork | 0.193 |
R-free | 0.25220 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4yfp |
RMSD bond length | 0.007 |
RMSD bond angle | 0.996 |
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] | 50.000 | 2.110 |
High resolution limit [Å] | 2.070 | 2.070 |
Rmerge | 0.078 | |
Rmeas | 0.130 | |
Rpim | 0.040 | 0.412 |
Number of reflections | 12510 | 1214 |
<I/σ(I)> | 26.2 | 1.9 |
Completeness [%] | 100.0 | 99.92 |
Redundancy | 10.4 | |
CC(1/2) | 0.815 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION, RECRYSTALLIZATION | 6.5 | 277 | PEG 3350, DL-malic acid |