28TN
Structure of a lambda repressor-like protein from Escherichia coli
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.2 |
| Synchrotron site | BESSY |
| Beamline | 14.2 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2025-07-23 |
| Detector | DECTRIS PILATUS3 6M |
| Wavelength(s) | 0.9184 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 60.216, 92.470, 160.387 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 46.230 - 2.110 |
| R-factor | 0.2152 |
| Rwork | 0.213 |
| R-free | 0.25920 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.442 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX (2.0_5936) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.240 | 2.240 |
| High resolution limit [Å] | 2.110 | 2.110 |
| Number of reflections | 37922 | 6269 |
| <I/σ(I)> | 5.99 | |
| Completeness [%] | 67.1 | 8.91 |
| Redundancy | 6.9 | 6.7 |
| CC(1/2) | 0.995 | 0.326 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 297.15 | 2 M (NH4)2SO4, 0.1 M Tris pH 8.5 |
