6NX3
Structures of the transcriptional regulator BgaR, a lactose sensor.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2018-07-14 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 1.458650 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 99.150, 46.317, 118.903 |
Unit cell angles | 90.00, 100.65, 90.00 |
Refinement procedure
Resolution | 46.860 - 1.870 |
R-factor | 0.22595 |
Rwork | 0.224 |
R-free | 0.25374 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 6nwh |
RMSD bond length | 0.008 |
RMSD bond angle | 1.470 |
Data reduction software | XDS |
Data scaling software | Aimless |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0238) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 48.250 | 1.900 |
High resolution limit [Å] | 1.870 | 1.870 |
Rmerge | 0.087 | 0.783 |
Rpim | 0.037 | 0.352 |
Number of reflections | 87904 | 4400 |
<I/σ(I)> | 9.4 | 2.4 |
Completeness [%] | 99.5 | 97.2 |
Redundancy | 6.6 | 5.9 |
CC(1/2) | 0.998 | 0.922 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 293 | 5 mg/mL protein; 20% PEG 3350, 200 mM MgCl2. Sitting drops were 200 nL plus 200 nL at 20C- no buffer was used in this crystallisation cocktail. |