2OL9
Peptide corresponding to residues 170-175 of human prion
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 8.2.2 |
| Synchrotron site | ALS |
| Beamline | 8.2.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-09-14 |
| Detector | ADSC QUANTUM 315 |
| Spacegroup name | P 1 |
| Unit cell lengths | 14.002, 4.879, 15.100 |
| Unit cell angles | 75.23, 75.88, 78.89 |
Refinement procedure
| Resolution | 14.290 - 0.850 |
| R-factor | 0.073 |
| Rwork | 0.073 |
| R-free | 0.07800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | idealized 6 residue beta strand |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.019 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 90.000 | 90.000 | 0.880 |
| High resolution limit [Å] | 0.850 | 1.830 | 0.850 |
| Rmerge | 0.036 | 0.027 | 0.078 |
| Number of reflections | 2681 | ||
| <I/σ(I)> | 48.7 | ||
| Completeness [%] | 82.1 | 96 | 33.5 |
| Redundancy | 3.6 | 3.8 | 2.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 298 | 200 mM Hepes, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
