5TCJ
Crystal structure of tryptophan synthase from M. tuberculosis - aminoacrylate and BRD4592-bound form
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2015-11-16 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.97934 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 135.092, 159.875, 165.331 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 2.400 |
| R-factor | 0.18082 |
| Rwork | 0.180 |
| R-free | 0.21074 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5tcf |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.291 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Refinement software | REFMAC (5.8.0155) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.440 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.138 | 0.000 |
| Number of reflections | 138958 | |
| <I/σ(I)> | 12.96 | 1.69 |
| Completeness [%] | 99.9 | 99.9 |
| Redundancy | 6.3 | 5.8 |
| CC(1/2) | 0.649 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 289 | 8% tacsimate pH 8.0, 20% PEG3350, 10 mM BaCl2, 1 mM BRD4592, soaked with 100 mM CsCl and 50 mM L-Ser, cryo 16% ethylene glycol |
