6NWO
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 | 2018-10-10 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.953723 |
| Spacegroup name | I 1 2 1 |
| Unit cell lengths | 68.429, 40.482, 261.721 |
| Unit cell angles | 90.00, 90.33, 90.00 |
Refinement procedure
| Resolution | 43.600 - 2.110 |
| R-factor | 0.19559 |
| Rwork | 0.194 |
| R-free | 0.23050 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 6nwh |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.427 |
| 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] | 43.620 | 2.170 |
| High resolution limit [Å] | 2.110 | 2.110 |
| Rmerge | 0.103 | 0.672 |
| Rpim | 0.043 | 0.290 |
| Number of reflections | 41261 | 3104 |
| <I/σ(I)> | 9.4 | 2.7 |
| Completeness [%] | 98.7 | 91.7 |
| Redundancy | 6.7 | 6.3 |
| CC(1/2) | 0.997 | 0.744 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 5.7 | 293 | 5 mg/mL protein; 21.7% PEG 3350, 222mM MgCl2, 100mM bis-tris pH 5.7. Sitting drops were set up in 200 nL plus 200 nL volumes at 20C |






