8DIR
The complex structure between human IgG1 Fc and its high affinity receptor FcgRI H174R variant
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2019-06-03 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 204.286, 89.276, 56.032 |
Unit cell angles | 90.00, 97.72, 90.00 |
Refinement procedure
Resolution | 36.870 - 2.300 |
R-factor | 0.198 |
Rwork | 0.196 |
R-free | 0.23280 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4x4m |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX (1.20.1_4487) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.340 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.070 | 0.464 |
Number of reflections | 44290 | 2235 |
<I/σ(I)> | 25.3 | 2.6 |
Completeness [%] | 99.8 | |
Redundancy | 6.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293 | 20% PEG3350, 0.2M Sodium Formate (pH6.6) |