4E1H
Fragment of human prion protein
Experimental procedure
Experimental method | SAD |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-C |
Synchrotron site | APS |
Beamline | 24-ID-C |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-11-27 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 1.73964 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 32.317, 42.898, 46.353 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 22.550 - 1.400 |
R-factor | 0.167 |
Rwork | 0.164 |
R-free | 0.21800 |
RMSD bond length | 0.016 |
RMSD bond angle | 1.751 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SHELX |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 30.000 | 30.000 | 1.450 |
High resolution limit [Å] | 1.400 | 3.020 | 1.400 |
Rmerge | 0.059 | 0.033 | 0.756 |
Number of reflections | 13272 | ||
<I/σ(I)> | 8.7 | ||
Completeness [%] | 99.8 | 98.8 | 100 |
Redundancy | 4.6 | 4.4 | 4.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 3.5 | 298 | 100mM Citrate pH 3.5, 10mM iron (II) chloride, and 25% PEG 3350, vapor diffusion, hanging drop, temperature 298K |
1 | VAPOR DIFFUSION, HANGING DROP | 3.5 | 298 | 100mM Citrate pH 3.5, 10mM iron (II) chloride, and 25% PEG 3350, vapor diffusion, hanging drop, temperature 298K |