3HAF
Human prion protein variant V129 domain swapped dimer
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-BM |
| Synchrotron site | APS |
| Beamline | 19-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-04-14 |
| Wavelength(s) | 0.9787 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 85.287, 86.358, 40.736 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 27.270 - 2.260 |
| R-factor | 0.206 |
| Rwork | 0.203 |
| R-free | 0.27800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.428 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | EPMR |
| Refinement software | REFMAC (5.5.0066) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 30.000 | 30.000 | 2.230 |
| High resolution limit [Å] | 2.150 | 4.630 | 2.150 |
| Rmerge | 0.086 | 0.047 | 0.378 |
| Number of reflections | 7351 | ||
| <I/σ(I)> | 3.889 | ||
| Completeness [%] | 83.4 | 99.9 | 40.2 |
| Redundancy | 5.5 | 5.7 | 2.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 10 | 293 | 0.1M Tris, 3.4M NaCl, pH 10.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
