6C52
Cross-alpha Amyloid-like Structure alphaTet
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.3.1 |
Synchrotron site | ALS |
Beamline | 8.3.1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2017-09-12 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 1.11584 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 47.450, 75.570, 27.990 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.185 - 1.600 |
R-factor | 0.1935 |
Rwork | 0.192 |
R-free | 0.22250 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.008 |
RMSD bond angle | 0.887 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | PHENIX ((1.12_2829: ???)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 76.000 | 1.650 |
High resolution limit [Å] | 1.600 | 1.600 |
Number of reflections | 25538 | 2532 |
<I/σ(I)> | 21.3 | 3.3 |
Completeness [%] | 98.9 | 97.6 |
Redundancy | 6.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 298 | 2.0 M Na formate, 0.1 M Na acetate |