6HTO
Tryptophan lyase 'empty state'
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID23-1 |
| Synchrotron site | ESRF |
| Beamline | ID23-1 |
| Temperature [K] | 100 |
| Detector technology | PIXEL |
| Collection date | 2018-03-10 |
| Detector | DECTRIS PILATUS 6M-F |
| Wavelength(s) | 0.98 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 46.970, 92.610, 94.460 |
| Unit cell angles | 90.00, 98.73, 90.00 |
Refinement procedure
| Resolution | 46.426 - 1.450 |
| R-factor | 0.1688 |
| Rwork | 0.168 |
| R-free | 0.19220 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4r34 |
| RMSD bond length | 0.012 |
| RMSD bond angle | 1.261 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | PHENIX ((1.13_2998: ???)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 47.000 | 1.490 |
| High resolution limit [Å] | 1.450 | 1.450 |
| Number of reflections | 257679 | 9677 |
| <I/σ(I)> | 15.25 | |
| Completeness [%] | 93.1 | |
| Redundancy | 5.29 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 298 | 14-20% PEG 3350, 0.2 M KBr, 1 mM 5'- deoxyadenosine (5'-dA), mM L-methionine, and 15 mg/mL SaNosL (protein buffer: 50 mM Tris pH 8; 150 mM NaCl and 2 mM DTT) |
