4QYP
The Crystal Structures of holo-wt human Cellular Retinol Binding protein II (hCRBPII) bound to Retinal
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 |
| Collection date | 2007-09-07 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 1 |
| Unit cell lengths | 36.440, 54.892, 68.716 |
| Unit cell angles | 107.75, 97.66, 103.08 |
Refinement procedure
| Resolution | 48.440 - 1.620 |
| R-factor | 0.20431 |
| Rwork | 0.202 |
| R-free | 0.25245 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2rcq |
| RMSD bond length | 0.025 |
| RMSD bond angle | 2.200 |
| Data reduction software | DENZO |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 50.000 |
| High resolution limit [Å] | 1.620 |
| Rmerge | 0.320 |
| Number of reflections | 56034 |
| Completeness [%] | 83.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 4.6 | 298 | 30% PEG 4000, 0.1 M sodium acetate, 0.1 M ammonium acetate , pH 4.6, EVAPORATION, temperature 298K |
