3BP6
Crystal structure of the mouse PD-1 Mutant and PD-L2 complex
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 | 2007-09-21 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9792 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 43.747, 84.335, 52.281 |
| Unit cell angles | 90.00, 108.00, 90.00 |
Refinement procedure
| Resolution | 23.980 - 1.600 |
| R-factor | 0.18583 |
| Rwork | 0.184 |
| R-free | 0.21833 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3bp5 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.251 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASES |
| Refinement software | REFMAC (5.3.0034) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 30.000 | 30.000 | 1.660 |
| High resolution limit [Å] | 1.600 | 3.450 | 1.600 |
| Rmerge | 0.054 | 0.033 | 0.405 |
| Number of reflections | 47813 | ||
| <I/σ(I)> | 16 | ||
| Completeness [%] | 99.7 | 99.7 | 99.5 |
| Redundancy | 5.3 | 6.2 | 4.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Sitting drop | 8.5 | 291 | 20% PEG 6000, 0.1 M Tris pH 8.5, Sitting drop, temperature 291K |
