4TUT
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 | 2010-11-18 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.72932 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 10.395, 9.731, 17.382 |
| Unit cell angles | 90.00, 105.94, 90.00 |
Refinement procedure
| Resolution | 9.996 - 0.900 |
| R-factor | 0.0712 |
| Rwork | 0.070 |
| R-free | 0.09800 |
| Structure solution method | AB INITIO PHASING |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.365 |
| Data reduction software | HKL-3000 |
| Data scaling software | SCALEPACK |
| Refinement software | PHENIX ((phenix.refine: 1.9_1692)) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 0.930 |
| High resolution limit [Å] | 0.900 | 1.940 | 0.900 |
| Rmerge | 0.066 | 0.067 | 0.068 |
| Total number of observations | 7403 | ||
| Number of reflections | 1862 | ||
| <I/σ(I)> | 27.4 | ||
| Completeness [%] | 71.4 | 92.5 | 32.3 |
| Redundancy | 4 | 5.4 | 1.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 0.1 M sodium cacodylate pH 6.5, 1.3 M sodium acetate, and 25 % ethylene glycol |
