8ALO
Heterodimer formation of sensory domains of Vibrio cholerae regulators ToxR and ToxS
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM30A |
Synchrotron site | ESRF |
Beamline | BM30A |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2016-12-08 |
Detector | DECTRIS EIGER X 4M |
Wavelength(s) | 0.967700 |
Spacegroup name | P 65 |
Unit cell lengths | 72.507, 72.507, 79.463 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 62.793 - 3.002 |
Rwork | 0.213 |
R-free | 0.25290 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | Alphafold Model |
RMSD bond length | 0.013 |
RMSD bond angle | 1.749 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0267) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 62.793 | 62.790 | 3.180 |
High resolution limit [Å] | 3.000 | 9.000 | 3.000 |
Rmerge | 0.108 | 0.034 | 0.842 |
Rmeas | 0.123 | 0.039 | 0.966 |
Rpim | 0.059 | 0.018 | 0.466 |
Number of reflections | 4790 | 183 | 756 |
<I/σ(I)> | 12.8 | ||
Completeness [%] | 100.0 | ||
Redundancy | 8.1 | 7.6 | 7.8 |
CC(1/2) | 0.999 | 0.999 | 0.688 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293.15 | 30mg/ml of ToxRSp in Tris buffer (20mM Tris, 150mM NaCl, pH7), 0.5 microliters of protein was mixed with 0.5 microliters of crystal condition (0.2 M Magnesium chloride hexahydrate. 0.1 M BIS-Tris. 5.5. 25 % w/v PEG 3350) |