6WDU
The external aldimine form of the Salmonella thypi wild-type tryptophan synthase in open conformation showing multiple side chain conformations for the residue beta Q114 and sodium ion at the metal coordination site. One of the beta-Q114 rotamer conformations allows a hydrogen bond to form with the PLP oxygen at the position 3 in the ring.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 12.3.1 |
| Synchrotron site | ALS |
| Beamline | 12.3.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2019-04-18 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.0000 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 182.655, 59.415, 67.345 |
| Unit cell angles | 90.00, 94.89, 90.00 |
Refinement procedure
| Resolution | 36.910 - 1.400 |
| R-factor | 0.1634 |
| Rwork | 0.162 |
| R-free | 0.19490 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4hn4 |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.526 |
| Data scaling software | SCALA (3.3.22) |
| Phasing software | PHASER (2.8.3) |
| Refinement software | REFMAC (5.8.0258) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 90.995 | 36.880 | 1.480 |
| High resolution limit [Å] | 1.398 | 4.430 | 1.400 |
| Rmerge | 0.042 | 0.920 | |
| Rmeas | 0.102 | 0.046 | 1.014 |
| Rpim | 0.042 | 0.018 | 0.418 |
| Total number of observations | 793906 | 27405 | 107971 |
| Number of reflections | 141196 | 4528 | 20297 |
| <I/σ(I)> | 9 | 23.7 | 1.5 |
| Completeness [%] | 99.6 | 97.5 | 98.4 |
| Redundancy | 5.6 | 6.1 | 5.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.8 | 293 | 50 mM Bicine-NaOH, 10% PEG 8,000, 2 mM Spermine, pH 7.8, 50mM NaCl |
