1F2Q
CRYSTAL STRUCTURE OF THE HUMAN HIGH-AFFINITY IGE RECEPTOR
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL7-1 |
Synchrotron site | SSRL |
Beamline | BL7-1 |
Temperature [K] | 110 |
Detector technology | IMAGE PLATE |
Collection date | 1998-06-11 |
Detector | MARRESEARCH |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 88.590, 69.640, 49.360 |
Unit cell angles | 90.00, 116.69, 90.00 |
Refinement procedure
Resolution | 17.430 - 2.400 |
R-factor | 0.226 |
Rwork | 0.226 |
R-free | 0.25400 |
RMSD bond length | 0.007 |
RMSD bond angle | 27.000 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | DM |
Refinement software | CNS (0.4) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.490 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.057 | 0.226 |
Number of reflections | 10247 | |
<I/σ(I)> | 23.8 | |
Completeness [%] | 96.8 | 92.5 |
Redundancy | 3.9 | 3.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 * | 297 | PEG 4000, Tris, Sodium Acetate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 297K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 20 (mM) | |
3 | 1 | reservoir | Tris-HCl | 100 (mM) | |
4 | 1 | reservoir | 200 (mM) | ||
5 | 1 | reservoir | PEG4000 | 18-24 (%) |