4N1E
Structural evidence for antigen receptor evolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 HF |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2011-12-15 |
| Detector | MAR scanner 345 mm plate |
| Wavelength(s) | 1.54179 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 114.917, 39.413, 178.301 |
| Unit cell angles | 90.00, 106.38, 90.00 |
Refinement procedure
| Resolution | 45.660 - 2.230 |
| R-factor | 0.225 |
| Rwork | 0.223 |
| R-free | 0.26450 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.452 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (3.3.16) |
| Phasing software | PHASER (2.3.0) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 171.061 | 45.664 | 2.330 |
| High resolution limit [Å] | 2.230 | 7.000 | 2.230 |
| Rmerge | 0.041 | 0.252 | |
| Total number of observations | 24553 | 35589 | |
| Number of reflections | 72711 | ||
| <I/σ(I)> | 14.3 | 14 | 3.1 |
| Completeness [%] | 93.5 | 99.7 | 76.3 |
| Redundancy | 6.2 | 9.2 | 4.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 293 | 0.2 M sodium formate, 18% (w/v) PEG3350, vapor diffusion, hanging drop, temperature 293K |
