3MD5
Prion peptide
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 | 2007-08-13 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.91840 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 19.618, 9.459, 19.672 |
Unit cell angles | 90.00, 92.92, 90.00 |
Refinement procedure
Resolution | 19.650 - 1.400 |
R-factor | 0.188 |
Rwork | 0.186 |
R-free | 0.23200 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.013 |
RMSD bond angle | 1.432 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | REFMAC (5.5.0088) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.450 |
High resolution limit [Å] | 1.400 | 3.020 | 1.400 |
Rmerge | 0.057 | 0.053 | 0.133 |
Number of reflections | 1309 | ||
<I/σ(I)> | 29.3 | ||
Completeness [%] | 84.1 | 93.6 | 61.7 |
Redundancy | 10.1 | 13.5 | 5.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 0.1 M Bis-Tris pH 6.5, 0.3 M ammonium acetate, 30-40% ethylene glycol, VAPOR DIFFUSION, SITTING DROP, temperature 293K |