6F2O
Crystal structure of mouse SALM5 adhesion protein extracellular LRR-Ig domain fragment
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID30B |
| Synchrotron site | ESRF |
| Beamline | ID30B |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-09-16 |
| Detector | DECTRIS EIGER R 4M |
| Wavelength(s) | 0.96770 |
| Spacegroup name | F 41 3 2 |
| Unit cell lengths | 254.015, 254.015, 254.015 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.940 - 3.000 |
| R-factor | 0.253 |
| Rwork | 0.252 |
| R-free | 0.28200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.360 |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | BALBES |
| Refinement software | BUSTER (2.10.2) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 3.180 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.133 | 2.226 |
| Number of reflections | 14488 | |
| <I/σ(I)> | 10.59 | 1.1 |
| Completeness [%] | 98.8 | 99.4 |
| Redundancy | 11.03 | 11.47 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5 | 283 | 20% PEG 1500 |
