7L1H
The aminoacrylate form of the wild-type Salmonella typhimurium Tryptophan Synthase in complex with inhibitor N-(4'-trifluoromethoxybenzenesulfonyl)-2-amino-1-ethylphosphate (F9F) at the enzyme alpha-site and cesium ion at the metal coordination site at 1.50 Angstrom resolution. Three water molecules are close to the amynoacrylate at the enzyme beta-site
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU MICROMAX-007 HF |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2020-03-05 |
| Detector | RIGAKU RAXIS IV++ |
| Wavelength(s) | 1.5418 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 183.970, 59.730, 67.420 |
| Unit cell angles | 90.00, 94.70, 90.00 |
Refinement procedure
| Resolution | 39.400 - 1.500 |
| R-factor | 0.1405 |
| Rwork | 0.138 |
| R-free | 0.18460 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4hn4 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.383 |
| Data reduction software | iMOSFLM (7.2.2) |
| Data scaling software | SCALA (3.3.22) |
| Phasing software | MOLREP (11.7.02) |
| Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 91.676 | 39.399 | 1.580 |
| High resolution limit [Å] | 1.500 | 4.740 | 1.500 |
| Rmerge | 0.054 | 0.039 | 0.263 |
| Rmeas | 0.063 | 0.046 | 0.344 |
| Rpim | 0.033 | 0.024 | 0.218 |
| Total number of observations | 13815 | 17433 | |
| Number of reflections | 104698 | 3827 | 7577 |
| <I/σ(I)> | 11.2 | 24.6 | 2.2 |
| Completeness [%] | 89.6 | 99.8 | 44.6 |
| Redundancy | 3.3 | 3.6 | 2.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.8 | 298 | 50 mM Bicine-CsOH, 10% PEG 8,000, 2 mM Spermine, pH 7.8 |
