3M45
Crystal structure of Ig1 domain of mouse SynCAM 2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X29A |
| Synchrotron site | NSLS |
| Beamline | X29A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-11-08 |
| Detector | ADSC QUANTUM 315 |
| Spacegroup name | P 1 |
| Unit cell lengths | 42.847, 50.528, 79.851 |
| Unit cell angles | 75.91, 77.02, 65.18 |
Refinement procedure
| Resolution | 50.000 - 2.210 |
| R-factor | 0.2 |
| Rwork | 0.198 |
| R-free | 0.24500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | A MONOMER OF HUMAN SYNCAM 3 (NECTIN-LIKE MOLECULE 1) IG1 PROTEIN DATA BANK CODE 1Z9M |
| RMSD bond length | 0.023 |
| RMSD bond angle | 2.234 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHASES |
| Refinement software | REFMAC (5.6.0031) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.260 |
| High resolution limit [Å] | 2.210 | 2.210 |
| Rmerge | 0.092 | 0.400 |
| Number of reflections | 27498 | |
| <I/σ(I)> | 15.27 | 3.39 |
| Completeness [%] | 93.9 | 64.1 |
| Redundancy | 3.6 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 293 | 0.1 M HEPES, pH 6.5-7.0, 21% PEG5000 monomethyl ether, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
