4U7L
LRIG1 extracellular domain: Structure and Function Analysis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
| Synchrotron site | Australian Synchrotron |
| Beamline | MX2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-09-25 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.954 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 38.940, 93.760, 169.430 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 48.378 - 2.300 |
| R-factor | 0.1968 |
| Rwork | 0.194 |
| R-free | 0.24780 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1xku |
| RMSD bond length | 0.004 |
| RMSD bond angle | 0.886 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX ((phenix.refine: 1.9_1692)) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 2.390 | ||
| High resolution limit [Å] | 2.300 | 7.140 | 2.300 |
| Rmerge | 0.132 | 0.045 | 2.242 |
| Rmeas | 0.143 | 0.050 | 2.412 |
| Total number of observations | 202942 | ||
| Number of reflections | 28430 | 1028 | 3003 |
| <I/σ(I)> | 9.21 | 27.27 | 0.87 |
| Completeness [%] | 99.8 | 94.8 | 99.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | EVAPORATION | 7 | 293 | 16% PEG4000 0.1M Hepes pH7.0 10mM Taurine |






