4QYN
The Crystal Structures of holo-wt human Cellular Retinol Binding protein II (hCRBPII) bound to Retinol
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 | IMAGE PLATE |
| Collection date | 2009-11-06 |
| Detector | MAR scanner 300 mm plate |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 34.650, 75.147, 54.650 |
| Unit cell angles | 90.00, 100.79, 90.00 |
Refinement procedure
| Resolution | 25.280 - 1.190 |
| R-factor | 0.18895 |
| Rwork | 0.187 |
| R-free | 0.21621 |
| Structure solution method | MOLECULAR REPLACEMENT |
| 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] | 1.190 |
| Number of reflections | 87302 |
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 |
