4W71
Crystal structure of a prion peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-07-01 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 1 |
| Unit cell lengths | 9.467, 10.382, 22.343 |
| Unit cell angles | 81.80, 81.40, 67.95 |
Refinement procedure
| Resolution | 10.997 - 1.000 |
| R-factor | 0.119 |
| Rwork | 0.118 |
| R-free | 0.15340 |
| Structure solution method | AB INITIO PHASING |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.327 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | SHELX |
| Refinement software | PHENIX ((phenix.refine: 1.9_1692)) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.040 |
| High resolution limit [Å] | 1.000 | 2.150 | 1.000 |
| Rmerge | 0.073 | 0.060 | 0.146 |
| Total number of observations | 7387 | ||
| Number of reflections | 3028 | ||
| <I/σ(I)> | 20.4 | ||
| Completeness [%] | 72.1 | 90.5 | 43 |
| Redundancy | 2.4 | 3.1 | 1.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 0.1 M Tris and 10-14 % ethanol |
