5CGQ
Crystal structure of Tryptophan Synthase from Salmonella typhimurium in complex with F9 ligand in the alpha-site and the product L-Tryptophan in the beta-site.
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 | 2012-05-04 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.0000 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 182.553, 59.300, 67.368 |
| Unit cell angles | 90.00, 94.82, 90.00 |
Refinement procedure
| Resolution | 39.210 - 1.180 |
| R-factor | 0.1414 |
| Rwork | 0.140 |
| R-free | 0.16050 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4ht3 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.406 |
| Data reduction software | MOSFLM (7.2.0) |
| Data scaling software | SCALA (3.3.22) |
| Phasing software | MOLREP (11.3.02) |
| Refinement software | REFMAC (5.8.0123) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 40.000 | 40.000 | 1.240 |
| High resolution limit [Å] | 1.180 | 3.730 | 1.180 |
| Rmerge | 0.081 | 0.037 | 0.872 |
| Rmeas | 0.086 | ||
| Rpim | 0.028 | 0.016 | 0.015 |
| Total number of observations | 2151280 | 64330 | 252941 |
| Number of reflections | 231646 | ||
| <I/σ(I)> | 14.7 | 39.6 | 3 |
| Completeness [%] | 98.6 | 98.4 | 94.2 |
| Redundancy | 9.3 | 8.5 | 7.9 |
| CC(1/2) | 0.999 | 0.999 | 0.778 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.6 | 298 | 50 mM Bicine-CsOH, pH 7.6, 10% PEG 8,000, 100 mM CsCl2, 1 mM spermine |
