3H9Y
Crystal structure of the IgE-Fc3-4 domains
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 5ID-B |
| Synchrotron site | APS |
| Beamline | 5ID-B |
| Temperature [K] | 113 |
| Detector technology | CCD |
| Collection date | 1998-08-30 |
| Detector | MAR CCD 130 mm |
| Wavelength(s) | 1.00796 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 153.676, 104.994, 49.222 |
| Unit cell angles | 90.00, 101.61, 90.00 |
Refinement procedure
| Resolution | 29.640 - 2.230 |
| R-factor | 0.23263 |
| Rwork | 0.231 |
| R-free | 0.26212 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Partially-refined monomer (chain C) from the IgE-Fc3-4 carbohydrate mutant P21 crystal form. |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.232 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER (1.3.1) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.380 |
| High resolution limit [Å] | 2.230 | 2.230 |
| Number of reflections | 36675 | |
| <I/σ(I)> | 20.943 | |
| Completeness [%] | 98.8 | 89.8 |
| Redundancy | 3.8 | 3.45 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.3 | 293 | 1 microliter of protein at 10 mg/mL in 20 mM sodium chloride was added to 1 microliter well solution (100 mM ammonium acetate, 100 mM sodium acetate pH 4.6, 30% (w/v) PEG 4000) and mixed by pipetting., VAPOR DIFFUSION, HANGING DROP, temperature 293K |
