7L03
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 sodium ion at the metal coordination site at 1.60 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 | 2020-08-18 |
Detector | RIGAKU RAXIS IV++ |
Wavelength(s) | 1.5418 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 182.490, 59.050, 67.245 |
Unit cell angles | 90.00, 95.02, 90.00 |
Refinement procedure
Resolution | 39.240 - 1.600 |
R-factor | 0.1731 |
Rwork | 0.171 |
R-free | 0.22420 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 4ht3 |
RMSD bond length | 0.009 |
RMSD bond angle | 1.627 |
Data reduction software | xia2 (0.5.902) |
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] | 90.895 | 39.238 | 1.690 |
High resolution limit [Å] | 1.599 | 5.060 | 1.600 |
Rmerge | 0.028 | 0.020 | 0.142 |
Rmeas | 0.038 | 0.027 | 0.193 |
Rpim | 0.023 | 0.017 | 0.120 |
Total number of observations | 7468 | 25175 | |
Number of reflections | 89582 | 3079 | 11579 |
<I/σ(I)> | 13.5 | 22.4 | 5.1 |
Completeness [%] | 95.4 | 99.3 | 85.2 |
Redundancy | 2.4 | 2.4 | 2.2 |
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 |