4WBU
prion peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-03-31 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.91840 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 9.439, 17.792, 44.561 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 22.280 - 1.150 |
| R-factor | 0.1507 |
| Rwork | 0.150 |
| R-free | 0.16650 |
| Structure solution method | AB INITIO PHASING |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.382 |
| 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 | 1.190 |
| High resolution limit [Å] | 1.150 | 2.480 | 1.150 |
| Rmerge | 0.102 | 0.081 | 0.186 |
| Total number of observations | 14648 | ||
| Number of reflections | 2627 | ||
| <I/σ(I)> | 11.1 | ||
| Completeness [%] | 87.6 | 90.5 | 65.2 |
| Redundancy | 5.6 | 7.2 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 0.1 M Hepes, 2.0 M ammonium sulfate, and 2.0 M NDSB-211 |
