3RJD
Crystal structure of Fc RI and its implication to high affinity immunoglobulin G binding
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 22-ID |
| Synchrotron site | APS |
| Beamline | 22-ID |
| Temperature [K] | 110 |
| Detector technology | CCD |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1 |
| Spacegroup name | P 32 2 1 |
| Unit cell lengths | 92.828, 92.828, 90.763 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 36.750 - 2.650 |
| R-factor | 0.25 |
| Rwork | 0.248 |
| R-free | 0.27600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.120 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | BALBES |
| Refinement software | BUSTER (2.8.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 40.000 | 2.860 |
| High resolution limit [Å] | 2.650 | 2.650 |
| Number of reflections | 13522 | |
| Completeness [%] | 99.9 | 98.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 295 | 10% PEG8000 and 10% PEG1000, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
