7RVC
Segment from the human prion protein 168-176 EYSNQNNFV
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ELECTRON MICROSCOPE |
| Source details | OTHER |
| Temperature [K] | 100 |
| Detector technology | CMOS |
| Collection date | 2016-11-13 |
| Detector | TVIPS TEMCAM-F416 |
| Wavelength(s) | 0.0251 |
| Spacegroup name | P 1 |
| Unit cell lengths | 10.020, 4.890, 31.330 |
| Unit cell angles | 90.99, 91.42, 102.18 |
Refinement procedure
| Resolution | 10.437 - 1.002 |
| R-factor | 0.1632 |
| Rwork | 0.163 |
| R-free | 0.16750 |
| Structure solution method | AB INITIO PHASING |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.607 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | SHELXD |
| Refinement software | PHENIX (1.12_2829) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 10.437 | 10.000 | 1.030 |
| High resolution limit [Å] | 1.000 | 4.480 | 1.000 |
| Rmerge | 0.187 | 0.103 | 0.432 |
| Rmeas | 0.207 | 0.114 | 0.492 |
| Total number of observations | 15771 | ||
| Number of reflections | 3031 | 30 | 167 |
| <I/σ(I)> | 5.56 | 10.16 | 2.11 |
| Completeness [%] | 97.6 | 85.7 | 77 |
| Redundancy | 5.203 | 5.233 | 4.102 |
| CC(1/2) | 0.988 | 0.990 | 0.840 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.5 | 298 | 20% ethanol, 0.1 M sodium acetate, pH 4.5, 0.1 M lithium sulfate |
