4MA7
Crystal structure of mouse prion protein complexed with Promazine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL9-2 |
Synchrotron site | SSRL |
Beamline | BL9-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-02-04 |
Detector | MARMOSAIC 325 mm CCD |
Wavelength(s) | 0.97946 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 83.211, 106.038, 75.733 |
Unit cell angles | 90.00, 95.68, 90.00 |
Refinement procedure
Resolution | 34.880 - 1.970 |
R-factor | 0.21741 |
Rwork | 0.216 |
R-free | 0.24687 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4h88 |
RMSD bond length | 0.005 |
RMSD bond angle | 1.082 |
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 | 1.970 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.090 | 0.620 |
Number of reflections | 52155 | |
<I/σ(I)> | 15.4 | 2 |
Completeness [%] | 98.3 | 85.1 |
Redundancy | 4.1 | 3.2 |
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 |