3CIQ
A regulatable switch mediates self-association in an immunoglobulin fold
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X12B |
Synchrotron site | NSLS |
Beamline | X12B |
Temperature [K] | 100 |
Spacegroup name | P 1 |
Unit cell lengths | 67.594, 68.047, 96.218 |
Unit cell angles | 104.38, 94.15, 117.77 |
Refinement procedure
Resolution | 50.000 - 2.900 |
R-factor | 0.2267 |
Rwork | 0.225 |
R-free | 0.26393 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.006 |
RMSD bond angle | 0.895 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 3.000 |
High resolution limit [Å] | 2.900 | 2.900 |
Rmerge | 0.079 | 0.363 |
Number of reflections | 28565 | |
Completeness [%] | 95.3 | 96.5 |
Redundancy | 2.2 | 2.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.4 | 288 | 28% PEG 3350, 200 mM ammonium tartrate dibasic, pH 7.40, VAPOR DIFFUSION, SITTING DROP, temperature 288K |