8URN
Crystal structure of EscI(51-87)-linker-EtgA(18-152) fusion protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | NSLS-II BEAMLINE 17-ID-1 |
Synchrotron site | NSLS-II |
Beamline | 17-ID-1 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2022-07-11 |
Detector | DECTRIS EIGER X 9M |
Wavelength(s) | 0.92010 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 107.629, 29.885, 74.564 |
Unit cell angles | 90.00, 118.19, 90.00 |
Refinement procedure
Resolution | 28.500 - 2.010 |
R-factor | 0.19145 |
Rwork | 0.189 |
R-free | 0.24472 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 1.459 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0415) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 28.500 | 2.082 |
High resolution limit [Å] | 2.010 | 2.010 |
Rmerge | 0.094 | 0.757 |
Number of reflections | 14194 | 905 |
<I/σ(I)> | 11.8 | 2.1 |
Completeness [%] | 99.0 | 88 |
Redundancy | 6.7 | 6.5 |
CC(1/2) | 0.998 | 0.709 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4.5 | 293 | 0.1 M sodium acetate pH 4.5 and 2 M ammonium sulfate |