4HPJ
Crystal structure of Tryptophan Synthase at 1.45 A resolution in complex with 2-aminophenol quinonoid in the beta site and the F9 inhibitor in the alpha 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 | 2012-05-11 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.000 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 184.329, 59.716, 67.527 |
| Unit cell angles | 90.00, 94.68, 90.00 |
Refinement procedure
| Resolution | 19.670 - 1.450 |
| R-factor | 0.1488 |
| Rwork | 0.147 |
| R-free | 0.18930 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1tjp |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.453 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (3.3.20) |
| Phasing software | MOLREP |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 91.858 | 19.789 | 1.530 |
| High resolution limit [Å] | 1.449 | 4.590 | 1.450 |
| Rmerge | 0.060 | 0.447 | |
| Total number of observations | 44173 | 30907 | |
| Number of reflections | 109585 | ||
| <I/σ(I)> | 13.1 | 9.9 | 1.6 |
| Completeness [%] | 84.8 | 96.4 | 62.9 |
| Redundancy | 7.7 | 10.9 | 2.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.8 | 298 | 50 mM Bicine-CsOH, 10% PEG 8,000, 2 mM Spermine, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
