3FEN
Crystal structure of the R132K:R111L:A32E mutant of cellular retinoic acid-binding protein II at 1.56 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] | 100 |
| Detector technology | CCD |
| Collection date | 2007-06-22 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 1.0000 |
| Spacegroup name | P 1 |
| Unit cell lengths | 34.692, 37.071, 58.549 |
| Unit cell angles | 102.55, 106.37, 92.87 |
Refinement procedure
| Resolution | 25.910 - 1.560 |
| R-factor | 0.15647 |
| Rwork | 0.154 |
| R-free | 0.19841 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2g7b |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.525 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 54.600 | 1.630 |
| High resolution limit [Å] | 1.560 | 1.560 |
| Rmerge | 0.064 | 0.221 |
| Number of reflections | 35378 | |
| <I/σ(I)> | 37.2 | 5.7 |
| Completeness [%] | 92.3 | 70.7 |
| Redundancy | 3.5 | 2.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 298 | 0.1M Tris, 0.2M NaOAc, 26% PEG4000, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
