4UBZ
Crystal structure of a prion peptide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-B |
Synchrotron site | APS |
Beamline | 23-ID-B |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-10-20 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.77490 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 11.609, 18.107, 17.843 |
Unit cell angles | 90.00, 105.24, 90.00 |
Refinement procedure
Resolution | 12.476 - 1.001 |
R-factor | 0.0886 |
Rwork | 0.088 |
R-free | 0.11040 |
Structure solution method | AB INITIO PHASING |
RMSD bond length | 0.006 |
RMSD bond angle | 1.358 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SHELX |
Refinement software | PHENIX ((phenix.refine: 1.9_1692)) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.040 |
High resolution limit [Å] | 1.000 | 2.150 | 1.000 |
Rmerge | 0.074 | 0.056 | 0.113 |
Total number of observations | 9659 | ||
Number of reflections | 3289 | ||
<I/σ(I)> | 14.4 | ||
Completeness [%] | 83.2 | 95.2 | 59.6 |
Redundancy | 2.9 | 3.9 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 293 | 0.2 M sodium thiocyanate and 2.2 M ammonium sulfate |