4R33
X-ray structure of the tryptophan lyase NosL with Tryptophan and S-adenosyl-L-homocysteine bound
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID23-2 |
Synchrotron site | ESRF |
Beamline | ID23-2 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2014-05-15 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 0.8726 |
Spacegroup name | P 1 2 1 |
Unit cell lengths | 94.720, 47.230, 114.360 |
Unit cell angles | 90.00, 108.71, 90.00 |
Refinement procedure
Resolution | 47.230 - 1.780 |
R-factor | 0.1597 |
Rwork | 0.159 |
R-free | 0.18130 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.010 |
RMSD bond angle | 1.156 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.9_1692)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 47.230 | 1.890 |
High resolution limit [Å] | 1.780 | 1.780 |
Number of reflections | 179387 | |
Completeness [%] | 1.0 | 0.983 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 298 | 14-20% PEG 3350; 200 mM KBr; 1 mM Tryptophan; 15 mg/mL protein, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 298K |