8CPL
YZw2 a scaffold for cryo-EM of small proteins of interest
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MAX IV BEAMLINE BioMAX |
Synchrotron site | MAX IV |
Beamline | BioMAX |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2022-07-02 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.976254 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 73.453, 173.903, 209.108 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 49.440 - 1.605 |
R-factor | 0.1888 |
Rwork | 0.188 |
R-free | 0.21030 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 1.010 |
Data reduction software | XDS |
Data scaling software | STARANISO |
Phasing software | PHASER |
Refinement software | BUSTER (2.10.4 (26-JUL-2023)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 49.440 | 1.751 |
High resolution limit [Å] | 1.600 | 1.605 |
Rmerge | 0.171 | 1.719 |
Rmeas | 0.178 | 1.788 |
Rpim | 0.048 | 0.485 |
Number of reflections | 203302 | 10164 |
<I/σ(I)> | 10 | 1.8 |
Completeness [%] | 58.4 | 12.8 |
Redundancy | 13.8 | 12.7 |
CC(1/2) | 0.996 | 0.618 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 16.6% w/v PEG3350, 0.2M NaF and 0.1M Bis-Tris Propane pH 5.5 |