6V67
Apo Structure of the De Novo PD-1 Binding Miniprotein GR918.2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-C |
| Synchrotron site | APS |
| Beamline | 24-ID-C |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2017-03-04 |
| Detector | DECTRIS PILATUS 6M-F |
| Wavelength(s) | 0.97911 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 50.849, 26.744, 51.537 |
| Unit cell angles | 90.00, 99.67, 90.00 |
Refinement procedure
| Resolution | 50.805 - 1.070 |
| R-factor | 0.1457 |
| Rwork | 0.145 |
| R-free | 0.14980 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Single helix residues 18-31 of the computational model |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.084 |
| Data reduction software | XDS (May 1, 2016) |
| Data scaling software | Aimless (0.5.23) |
| Phasing software | PHASER (2.7.18) |
| Refinement software | PHENIX (dev_2849) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.810 | 50.810 | 1.030 |
| High resolution limit [Å] | 1.020 | 5.470 | 1.020 |
| Rmerge | 0.059 | 0.042 | 0.593 |
| Rmeas | 0.067 | 0.048 | 0.785 |
| Rpim | 0.031 | 0.021 | 0.508 |
| Total number of observations | 138087 | 1169 | 1556 |
| Number of reflections | 33643 | 258 | 1093 |
| <I/σ(I)> | 10.7 | 28.2 | 1 |
| Completeness [%] | 95.0 | 99.3 | 60.8 |
| Redundancy | 4.1 | 4.5 | 1.4 |
| CC(1/2) | 0.998 | 0.996 | 0.652 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293.15 | 0.1 M MES/Imidazole pH 6.5, 0.03 M Diethylene Glycol, 0.03 M Triethylene Glycol, 0.03 M Tetraethylene Glycol, 0.03 M Pentaethylene Glycol, 10% PEG 20,000, 20% PEG MME 550 |
