8X2T
The Crystal Structure of FES from Biortus.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | CLSI BEAMLINE 08ID-1 |
Synchrotron site | CLSI |
Beamline | 08ID-1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2023-07-14 |
Detector | DECTRIS EIGER X 9M |
Wavelength(s) | 0.979514 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 191.882, 29.952, 73.792 |
Unit cell angles | 90.00, 107.67, 90.00 |
Refinement procedure
Resolution | 45.748 - 2.900 |
Rwork | 0.270 |
R-free | 0.33940 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.001 |
RMSD bond angle | 1.108 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 45.750 | 2.980 |
High resolution limit [Å] | 2.900 | 2.900 |
Rmerge | 0.014 | 0.385 |
Number of reflections | 8125 | 1352 |
<I/σ(I)> | 9.9 | |
Completeness [%] | 87.8 | |
Redundancy | 5.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 0.2M CaCl2, 0.1M Tris pH8.5, 25% PEG 4000 |