5LBM
The asymmetric tetrameric structure of the formaldehyde sensing transcriptional repressor FrmR from Escherichia coli
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | DIAMOND BEAMLINE I03 |
| Synchrotron site | Diamond |
| Beamline | I03 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2016-02-08 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.9763 |
| Spacegroup name | P 31 |
| Unit cell lengths | 82.069, 82.069, 55.251 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 55.250 - 2.700 |
| R-factor | 0.2117 |
| Rwork | 0.209 |
| R-free | 0.26628 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.598 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0151) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 55.250 | 2.830 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.499 | |
| Rpim | 0.038 | 0.499 |
| Number of reflections | 11450 | |
| <I/σ(I)> | 12.2 | 2.2 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 5.3 | 5.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 290 | 0.2 M MgCl2, 0.1 M Na cacodylate pH 6.5 and 31 % PEG 2000 Protein buffered in: 50mM Hepes pH 7.5 and 0.5 M NaCl |
