7KYT
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, cesium ion at the metal coordination site and benzimidazole (BZI) at the enzyme beta-site at 1.35 Angstrom resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-C |
Synchrotron site | APS |
Beamline | 24-ID-C |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2020-02-05 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 1.000000 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 184.460, 61.250, 67.560 |
Unit cell angles | 90.00, 94.57, 90.00 |
Refinement procedure
Resolution | 19.570 - 1.350 |
R-factor | 0.1763 |
Rwork | 0.174 |
R-free | 0.20860 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 7kxc |
RMSD bond length | 0.007 |
RMSD bond angle | 1.343 |
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] | 91.937 | 19.566 | 1.420 |
High resolution limit [Å] | 1.350 | 4.270 | 1.350 |
Rmerge | 0.078 | 0.024 | 0.838 |
Rmeas | 0.108 | 0.037 | 1.106 |
Rpim | 0.058 | 0.019 | 0.600 |
Total number of observations | 16708 | 76845 | |
Number of reflections | 162194 | 4768 | 23532 |
<I/σ(I)> | 5.7 | 16.2 | 1.1 |
Completeness [%] | 98.7 | 89 | 98.6 |
Redundancy | 3.3 | 3.5 | 3.3 |
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 |