4EFG
Crystal Structure of the Q108K:K40L:T51V:T53C:Y19W:R58W:T29L Mutant of Cellular Retinol Binding Protein Type II in Complex with All-trans-Retinal at 1.58 Angstrom Resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-D |
Synchrotron site | APS |
Beamline | 21-ID-D |
Temperature [K] | 200 |
Detector technology | CCD |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1.1272 |
Spacegroup name | P 1 |
Unit cell lengths | 30.111, 35.905, 64.726 |
Unit cell angles | 90.93, 91.21, 114.13 |
Refinement procedure
Resolution | 28.910 - 1.580 |
R-factor | 0.19644 |
Rwork | 0.194 |
R-free | 0.24154 |
Structure solution method | MOLREP |
Starting model (for MR) | 2rcq |
RMSD bond length | 0.023 |
RMSD bond angle | 2.099 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 28.910 | |
High resolution limit [Å] | 1.580 | 1.580 |
Number of reflections | 33875 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION, RECRYSTALLIZATION | 4.6 | 298 | 40% PEG4000, 0.1 M sodium acetate trihydrate, pH 4.6, 0.1 M ammonium acetate, EVAPORATION, RECRYSTALLIZATION, temperature 298K |