7RVL
Segment from the Y169F mutant of the human prion protein 168-176 EFSNQNNFV
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ELECTRON MICROSCOPE |
Source details | OTHER |
Temperature [K] | 100 |
Detector technology | CMOS |
Collection date | 2017-04-25 |
Detector | TVIPS TEMCAM-F416 |
Wavelength(s) | 0.0251 |
Spacegroup name | P 1 |
Unit cell lengths | 4.900, 10.380, 30.260 |
Unit cell angles | 90.91, 90.82, 102.25 |
Refinement procedure
Resolution | 10.140 - 1.000 |
R-factor | 0.1915 |
Rwork | 0.190 |
R-free | 0.21060 |
Structure solution method | AB INITIO PHASING |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | SHELXD |
Refinement software | PHENIX (1.19.2_4158) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 10.140 | 10.140 | 1.030 |
High resolution limit [Å] | 1.000 | 4.470 | 1.000 |
Rmerge | 0.178 | 0.097 | 0.363 |
Rmeas | 0.197 | 0.107 | 0.400 |
Total number of observations | 14661 | ||
Number of reflections | 2737 | 29 | 163 |
<I/σ(I)> | 5.99 | 10.18 | 3.66 |
Completeness [%] | 87.1 | 80.6 | 69.7 |
Redundancy | 5.357 | 5.517 | 5.006 |
CC(1/2) | 0.985 | 0.986 | 0.940 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 4.5 | 298 | 0.1 M sodium acetate, pH 4.5, 1 M sodium chloride, 0.1 M lithium sulfate |