2RGS
FC-fragment of monoclonal antibody IGG2B from Mus musculus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-06-15 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.9168 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 138.946, 63.956, 72.624 |
| Unit cell angles | 90.00, 103.83, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.130 |
| R-factor | 0.20148 |
| Rwork | 0.201 |
| R-free | 0.21300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | FC-FRAGMENT OF PDB ENTRY 1IGT |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.555 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.160 |
| High resolution limit [Å] | 2.100 | 2.100 |
| Rmerge | 0.113 | 0.449 |
| Number of reflections | 34014 | |
| <I/σ(I)> | 10.3 | 2.91 |
| Completeness [%] | 97.9 | 100 |
| Redundancy | 3.3 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 301 | 20% PEG2000, 0.1 M HEPES pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 301K |
