6C97
Crystal structure of FcRn at pH3
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CLSI BEAMLINE 08ID-1 |
Synchrotron site | CLSI |
Beamline | 08ID-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-10-02 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97949 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 42.100, 76.250, 140.150 |
Unit cell angles | 90.00, 93.75, 90.00 |
Refinement procedure
Resolution | 46.616 - 2.000 |
R-factor | 0.1756 |
Rwork | 0.174 |
R-free | 0.21020 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 0.897 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Refinement software | PHENIX ((DEV_2443: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.050 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.076 | 0.545 |
Number of reflections | 59210 | 4328 |
<I/σ(I)> | 10.91 | 2.39 |
Completeness [%] | 98.8 | 98.9 |
Redundancy | 3 | 3 |
CC(1/2) | 0.997 | 0.676 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 3 | 289 | APO FCRN CRYSTALS WERE PRODUCED BY SITTING DROP VAPOR DIFFUSION WITH AN EQUAL VOLUME COMBINATION OF THE PROTEIN COMPLEX, PROVIDED IN A PROTEIN SOLUTION CONTAINING 50MM HEPES PH 7.0 AND 75MM NACL, AND AN OPTIMIZATION SCREEN CONTAINING 0.1M CITRIC ACID/NAOH PH 3.01-3.09 AND 12-16% W/V PEG 6,000. |