3HER
Human prion protein variant F198S with V129
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Collection date | 2008-03-06 |
| Wavelength(s) | 0.9786 |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 57.611, 57.611, 163.337 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 28.810 - 1.850 |
| R-factor | 0.227 |
| Rwork | 0.226 |
| R-free | 0.26500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.409 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0066) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.920 |
| High resolution limit [Å] | 1.850 | 3.990 | 1.850 |
| Rmerge | 0.039 | 0.025 | 0.447 |
| Number of reflections | 24056 | ||
| <I/σ(I)> | 33.439 | ||
| Completeness [%] | 91.7 | 98.7 | 86.2 |
| Redundancy | 5.8 | 8.5 | 5.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 293 | 0.1 M Tris, 0.2 M Mg acetate, 8% PEG 6K, 5 mM CdCl2, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
