4E1I
Fragment of human prion protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU MICROMAX-007 HF |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-10-13 |
Detector | RIGAKU SATURN 944+ |
Wavelength(s) | 1.5418 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 35.338, 41.217, 46.600 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 23.300 - 2.030 |
R-factor | 0.19 |
Rwork | 0.187 |
R-free | 0.25300 |
RMSD bond length | 0.012 |
RMSD bond angle | 1.225 |
Data scaling software | SCALA (3.3.16) |
Phasing software | PHASER (2.1.4) |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 30.873 | 41.217 | 2.140 |
High resolution limit [Å] | 2.028 | 6.410 | 2.028 |
Rmerge | 0.038 | 0.196 | |
Total number of observations | 914 | 2312 | |
Number of reflections | 4685 | ||
<I/σ(I)> | 20.1 | 16.1 | 3.9 |
Completeness [%] | 98.6 | 98.4 | 90.7 |
Redundancy | 5.7 | 5 | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 298 | 100mM Bis Tris pH 5.5, 25% PEG 3350, vapor diffusion, hanging drop, temperature 298K |