3MD4
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 | 2007-03-31 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.91840 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 9.439, 17.792, 44.561 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 22.280 - 1.150 |
R-factor | 0.15 |
Rwork | 0.149 |
R-free | 0.16900 |
Structure solution method | AB INITIO PHASING |
RMSD bond length | 0.015 |
RMSD bond angle | 1.454 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHELXD |
Refinement software | REFMAC (5.5.0088) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.190 |
High resolution limit [Å] | 1.150 | 2.480 | 1.150 |
Rmerge | 0.102 | 0.081 | 0.186 |
Number of reflections | 2627 | ||
<I/σ(I)> | 11.1 | ||
Completeness [%] | 87.6 | 90.5 | 65.2 |
Redundancy | 5.6 | 7.2 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | 0.1 M HEPES pH 7.5, 2.0 M ammonium sulfate, VAPOR DIFFUSION, SITTING DROP, temperature 293K |