4EDE
Crystal Structure of the Q108K:K40L:T51V:T53C:Y19W:R58W:T29L:A33W Mutant of Cellular Retinol Binding Protein Type II in Complex with All-trans-Retinal at 1.4 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) | 0.97918 |
| Spacegroup name | P 1 |
| Unit cell lengths | 31.348, 36.452, 64.265 |
| Unit cell angles | 90.04, 94.55, 116.36 |
Refinement procedure
| Resolution | 32.637 - 1.400 |
| R-factor | 0.20159 |
| Rwork | 0.199 |
| R-free | 0.24158 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2rcq |
| RMSD bond length | 0.029 |
| RMSD bond angle | 2.434 |
| 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] | 32.637 | 1.420 |
| High resolution limit [Å] | 1.400 | 1.400 |
| Rmerge | 0.358 | |
| Number of reflections | 49822 | |
| <I/σ(I)> | 2.7 | |
| Completeness [%] | 93.5 |
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 |
