4MA8
Crystal structure of mouse prion protein complexed with Chlorpromazine
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 | 2012-12-06 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.007 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 83.262, 106.883, 75.594 |
| Unit cell angles | 90.00, 95.32, 90.00 |
Refinement procedure
| Resolution | 34.990 - 2.200 |
| R-factor | 0.19664 |
| Rwork | 0.195 |
| R-free | 0.23585 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4h88 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.322 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.280 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.080 | 0.570 |
| Number of reflections | 32491 | |
| <I/σ(I)> | 14 | 1.5 |
| Completeness [%] | 97.3 | 86.4 |
| Redundancy | 3.5 | 2.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 298 | 25% PEG3350, 0.1 M Bis-Tris, pH 6.5, 0.2 M lithium sulfate, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
