9E2B
Structure of a solute binding protein from Desulfonauticus sp. bound to L-tryptophan
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 | 2024-10-03 |
| Detector | DECTRIS EIGER X 16M |
| Wavelength(s) | 0.9537 |
| Spacegroup name | P 1 |
| Unit cell lengths | 74.507, 74.593, 92.348 |
| Unit cell angles | 98.21, 91.24, 119.84 |
Refinement procedure
| Resolution | 39.140 - 1.800 |
| R-factor | 0.1866 |
| Rwork | 0.185 |
| R-free | 0.21610 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.007 |
| RMSD bond angle | 0.886 |
| Data reduction software | XDS |
| Data scaling software | Aimless |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.20.1_4487: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 39.140 | 1.830 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.089 | 1.254 |
| Rmeas | 0.104 | 1.461 |
| Rpim | 0.054 | 0.746 |
| Total number of observations | 568516 | 28491 |
| Number of reflections | 153832 | 7559 |
| <I/σ(I)> | 7.6 | 0.8 |
| Completeness [%] | 97.8 | |
| Redundancy | 3.7 | 3.8 |
| CC(1/2) | 0.993 | 0.484 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 291 | 27% PEG 3350, 0.1M sodium acetate pH 4.5 |
