7QSQ
Permutated N-terminal lobe of the ribose binding protein from Thermotoga maritima
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.1 |
| Synchrotron site | BESSY |
| Beamline | 14.1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2019-09-26 |
| Detector | DECTRIS PILATUS 6M |
| Wavelength(s) | 0.9184 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 55.370, 62.770, 76.260 |
| Unit cell angles | 90.00, 102.09, 90.00 |
Refinement procedure
| Resolution | 48.960 - 1.790 |
| R-factor | 0.1933 |
| Rwork | 0.191 |
| R-free | 0.23860 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2fn9 |
| RMSD bond length | 0.003 |
| RMSD bond angle | 0.571 |
| Data reduction software | XDS (20210323) |
| Data scaling software | XDS (20210323) |
| Phasing software | PHASER (2.8.3) |
| Refinement software | PHENIX (1.19.2_4158) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 48.960 | 1.860 |
| High resolution limit [Å] | 1.790 | 1.790 |
| Rmerge | 0.080 | 1.324 |
| Rmeas | 0.094 | 1.548 |
| Rpim | 0.047 | 0.788 |
| Number of reflections | 47556 | 4346 |
| <I/σ(I)> | 8.58 | 0.76 |
| Completeness [%] | 97.8 | 85.5 |
| Redundancy | 3.7 | 3.6 |
| CC(1/2) | 0.997 | 0.413 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293 | 30% PEG 4000, 0.2 M Lithium-sulfate, 0.1 M Tris pH 8.0, 4% 2,2,2-Trifluoroethanol |
